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PID QueryLength Homolgous Sequence in PDB UniProt Query TITLE
35587 794 210 P09958(FURIN_HUMAN) RecName: Full=Furin; EC=3.4.21.75 {ECO:0000269|PubMed:11799113, ECO:0000269|PubMed:1629222, ECO:0000269|PubMed:1713771, ECO:0000269|PubMed:2251280, ECO:0000269|PubMed:25974265, ECO:0000269|PubMed:7592877, ECO:0000269|PubMed:7690548, ECO:0000269|PubMed:9130696};AltName: Full=Dibasic-processing enzyme;AltName: Full=Paired basic amino acid residue-cleaving enzyme; Short=PACE;Flags: Precursor;
QUERYSEQ
MELRPWLLWVVAATGTLVLLAADAQGQKVFTNTWAVRIPGGPAVANSVARKHGFLNLGQIFGDYYHFWHRGVTKRSLSPHRPRHSRLQREPQVQWLEQQVAKRRTKRDVYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIVVS
ILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQMNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLDGEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPARLAEEAFFRGVSQGRGGLGSIFVWASGNGGREH
DSCNCDGYTNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNEKQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNLTWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGLLDAGAMVALAQNWTTVAPQRKC
IIDILTEPKDIGKRLEVRKTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSPMGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWVLEIENTSEANNYGTLTKFTLVLYGTAPEGLPVPPESSGCKTLTSSQACVVCE
EGFSLHQKSCVQHCPPGFAPQVLDTHYSTENDVETIRASVCAPCHASCATCQGPALTDCLSCPSHASLDPVEQTCSRQSQSSRESPPQQQPPRLPPEVEAGQRLRAGLLPSHLPEVVAGLSCAFIVLVFVTVFLVLQLRSGFSFRGVKVY
TMDRGLISYKGLPPEAWQEECPSDSEEDEGRGERTAFIKDQSAL
[BLAST file for PDB] (plain) (bar) (multiple alignment) [BLAST for UniProt: (plain) (bar) (multiple alignment) (PSSM file) ]

UniProt Feature Tables [P09958(FURIN_HUMAN)]

794
region name description
1-26 SIGNAL
27-107 PROPEP /note="Inhibition peptide" /id="PRO_0000027028"
108-794 CHAIN /note="Furin" /id="PRO_0000027029"
108-715 TOPO_DOM /note="Lumenal"
716-738 TRANSMEM /note="Helical"
739-794 TOPO_DOM /note="Cytoplasmic"
121-435 DOMAIN /note="Peptidase S8"
444-576 DOMAIN /note="P/Homo B"
577-620 REPEAT /note="FU 1"
638-681 REPEAT /note="FU 2"
191-192 REGION /note="Substrate binding" ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265"
253-258 REGION /note="Substrate binding" ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265"
292-295 REGION /note="Substrate binding" ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265"
759-762 REGION /note="Cell surface signal"
153-153 ACT_SITE /note="Charge relay system"
194-194 ACT_SITE /note="Charge relay system"
368-368 ACT_SITE /note="Charge relay system"
115-115 METAL /note="Calcium 1" ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265"
162-162 METAL /note="Calcium 1" ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265"
174-174 METAL /note="Calcium 2" ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265"
179-179 METAL /note="Calcium 2" ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265"
181-181 METAL /note="Calcium 2; via carbonyl oxygen" ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265"
205-205 METAL /note="Calcium 1; via carbonyl oxygen" ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265"
208-208 METAL /note="Calcium 1" ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265"
210-210 METAL /note="Calcium 1; via carbonyl oxygen" ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265"
212-212 METAL /note="Calcium 1; via carbonyl oxygen" ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265"
258-258 METAL /note="Calcium 3" ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265"
301-301 METAL /note="Calcium 3" ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265"
331-331 METAL /note="Calcium 3" ECO:0000244|PDB:4RYD, ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265"
154-154 BINDING /note="Substrate" ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265"
236-236 BINDING /note="Substrate" ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265"
264-264 BINDING /note="Substrate" ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265"
306-306 BINDING /note="Substrate" ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265"
308-308 BINDING /note="Substrate" ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265"
368-368 BINDING /note="Substrate" ECO:0000244|PDB:4RYD, ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265"
1-794 DISORDER predicted by DISOPRED (1-23,78-79,365-367,369-373,579-591,678-694,696-698,769-794)

MONOMER
794
pdb_id a1 identity[%]2 description
5jmo B 99.4 FURIN_HUMAN Furin
6a8y A 100.0 FURIN_HUMAN YR26_SDS
3whi B 35.7 SUBT_BACSU Subtilisin E
1kn6 A 38.6 NEC1_MOUSE Prohormone Convertase 1
1.a1:asym_id for the homologue. 2.identity[%]2:sequence identity between the query and the homologue.
HETERO
794 pdb_id contact mol homologue
a3 description a4 identity[%]5 Ncon6 description
6hlb[1] B PHE-(ALN)-ARG-ARG-ARG-ARG-SLL-ARG-00S[7 aa] A 100.0
/100.0
27
/27
FURIN_HUMAN Furin
5jmo[2] C camelid VHH fragment[115 aa] A 100.0
/99.4
15
/15
FURIN_HUMAN Furin
6hzd[1] B ARG-ARG-ARG-LYS-ARG-00S[6 aa] A 100.0
/99.4
28
/28
FURIN_HUMAN Furin
6hle[2] B LYS-ARG-ARG-TBG-LYS-00S[6 aa] A 100.0
/99.4
26
/26
FURIN_HUMAN Furin
6hza[1] B ARG-ARG-LYS-ARG-00S[5 aa] A 100.0
/99.4
27
/27
FURIN_HUMAN Furin
6eqv[1] B HY1-LLI-VAL-ARG-00S[5 aa] A 100.0
/99.4
25
/25
FURIN_HUMAN Furin
4ryd[7] H para-guanidinomethyl-phenylacetyl-Arg-(3-methylval.. B 100.0
/100.0
26
/26
FURIN_HUMAN Furin
6hld[1] B ALN-ARG-ARG-ARG-SLL-LYS-00S[7 aa] A 100.0
/99.4
27
/27
FURIN_HUMAN Furin
6hzb[1] B ARG-ARG-LYS-LYS-00S[5 aa] A 100.0
/99.4
28
/28
FURIN_HUMAN Furin
4omd[14] H phenylacetyl-Arg-Val-Arg-(amidomethyl)benzamidine[.. B 100.0
/100.0
23
/23
FURIN_HUMAN Furin
6eqx[1] B Arg-Arg-Arg-Val-Arg-00S[6 aa] A 100.0
/99.4
28
/28
FURIN_HUMAN Furin
1p8j[11] K DECANOYL-ARG-VAL-LYS-ARG-CHLOROMETHYLKETONE INHIBI.. C 100.0
/97.9
25
/25
FURI_MOUSE Furin precursor
1p8j[4] K DECANOYL-ARG-VAL-LYS-ARG-CHLOROMETHYLKETONE INHIBI.. B 100.0
/97.9
4
/4
FURI_MOUSE Furin precursor
4hx2[2] B Q9FDS0_STRCS Neutral proteinase inhibitor ScNPI[114 aa] A 100.0
/49.2
1
/21
Q9FDF2_BACLI KerA
3qtl[2] D A1X1V8_CARRO Kazal-type serine protease inhibitor SPI-1[75 aa] A 100.0
/49.2
1
/21
Q1EM64_BACLI Subtilisin-like serin protease
4gi3[1] B SPI_SCHGR Greglin[57 aa] A 100.0
/49.2
1
/21
Q9FDF2_BACLI KerA
1oyv[2] C IP21_LYCES Wound-induced proteinase inhibitor-II[104 aa] A 50.0
/49.2
2
/27
SUBT_BACLI Subtilisin Carlsberg
1sib[5] B ICIC_HIRME EGLIN C[63 aa] A 60.0
/40.9
5
/23
SUBT_BACAM SUBTILISIN NOVO BPN'
3tec[3] B ICIC_HIRME EGLIN C[63 aa] A 75.0
/44.7
4
/27
THET_THEVU THERMITASE
1r0r[3] B IOVO_MELGA Ovomucoid[51 aa] A 50.0
/49.2
2
/23
SUBT_BACLI subtilisin carlsberg
5ox2[1] B Fragment of prodomain[9 aa] A 100.0
/48.6
1
/15
SUBT_BACAM Subtilisin BPN'
3cnq[3] A SUBT_BACAM Subtilisin BPN' [71 aa] B 100.0
/47.1
1
/37
SUBT_BACAM Subtilisin BPN'
1sua[1] B TETRAPEPTIDE ALA-LEU-ALA-LEU[4 aa] A 100.0
/47.1
1
/16
SUBT_BACAM SUBTILISIN BPN'
1spb[1] A SUBT_BACAM SUBTILISIN BPN' PROSEGMENT [71 aa] B 100.0
/45.7
1
/34
SUBT_BACAM SUBTILISIN BPN'
2id4[2] C Ac-RERK-CMK inhibitor[6 aa] A 68.4
/42.3
19
/19
KEX2_YEAST Kexin
1ot5[2] D Ac-Ala-Lys-boroArg N-acetylated boronic acid pepti.. B 94.4
/42.2
18
/18
KEX2_YEAST Kexin
1r64[2] C Ac-Arg-Glu-Lys-boroArg peptide inhibitor[5 aa] A 83.3
/42.2
24
/24
KEX2_YEAST Kexin
2sni[32] B ICI2_HORVU CHYMOTRYPSIN INHIBITOR 2[64 aa] A 66.7
/40.9
3
/22
SUBT_BACAM SUBTILISIN NOVO
3sic[6] B SSI_STRAO STREPTOMYCES SUBTILISIN INHIBITOR (SSI)[107 aa] A 66.7
/40.9
3
/26
SUBT_BACAM SUBTILISIN BPN'
1v5i[1] B PIA1_PLEOS IA-1=serine proteinase inhibitor[76 aa] A 100.0
/40.9
2
/26
SUBT_BACAM Subtilisin BPN'
1scj[1] B SUBT_BACSU SUBTILISIN E[71 aa] A 50.0
/40.7
2
/32
SUBT_BACSU SUBTILISIN E
3bx1[4] D IAAS_HORVU Alpha-amylase/subtilisin inhibitor[181 aa] B 38.5
/37.0
13
/16
SUBS_BACLE Subtilisin Savinase
3bx1[2] D IAAS_HORVU Alpha-amylase/subtilisin inhibitor[181 aa] A 25.0
/37.0
8
/10
SUBS_BACLE Subtilisin Savinase
3bx1[4] C IAAS_HORVU Alpha-amylase/subtilisin inhibitor[181 aa] B 38.5
/37.0
26
/26
SUBS_BACLE Subtilisin Savinase
1tk2[1] B GRAMICIDIN S[10 aa] A 38.5
/37.0
13
/13
SUBS_BACLE SUBTILISIN SAVINASE
5yl7[1] B Copurified unknown peptide[3 aa] A 55.6
/31.1
9
/9
Pseudoalteromonas arctica PAMC 21717
3wqb[1] B Open reading frame 2[99 aa] A 33.3
/31.0
27
/35
Q9L5A4_AERSO Extracellular serine protease
2b6n[1] B TRIPEPTIDE[3 aa] A 50.0
/29.7
8
/8
Q3HUQ2_9ENTR proteinase K
4lvn[2] D Q868D6_PLAFA Subtilisin-like serine protease[81 aa] A 23.1
/26.9
26
/28
Q868D6_PLAFA Subtilisin-like serine protease
4lvn[2] B NIMP.M7 Fab light chain[207 aa] A 0.0
/26.9
2
/7
Q868D6_PLAFA Subtilisin-like serine protease
3.a3:asym_id for the contact molecule. 4.a4:asym_id for the template homologue. 5.identity[%]5:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon6:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.
COMPOUND
794 pdb_id contact mol homologue
a3 description a4 identity[%]5 Ncon6 description
6hzb[3] M PTD
PENTANEDIAL[7 atoms]
A 100.0
/99.4
1
/1
FURIN_HUMAN Furin
6hzc[1] M PTD
PENTANEDIAL[7 atoms]
A 100.0
/99.4
5
/5
FURIN_HUMAN Furin
6hle[1] M GEB
3-[4-(3-oxidanylidenepropyl)piperazin-1-yl]propana..
A 100.0
/99.4
4
/4
FURIN_HUMAN Furin
6hzc[1] N BVK
2-[4-(aminomethyl)phenyl]ethanoic acid[11 atoms]
A 100.0
/99.4
1
/1
FURIN_HUMAN Furin
5mim[1] K 1N
1-[(1~{R},2~{R},4~{S},5~{S})-2,4-bis(4-carbamimida..
A 100.0
/99.4
14
/14
FURIN_HUMAN Furin
5mim[1] J 1N
1-[(1~{R},2~{R},4~{S},5~{S})-2,4-bis(4-carbamimida..
A 100.0
/99.4
7
/7
FURIN_HUMAN Furin
1r64[1] H NAG
2-acetamido-2-deoxy-beta-D-glucopyranose[14 atoms]..
A 57.1
/42.2
7
/7
KEX2_YEAST Kexin
2id4[2] L NAG
2-acetamido-2-deoxy-beta-D-glucopyranose[14 atoms]..
B 0.0
/42.3
1
/1
KEX2_YEAST Kexin
5jmo[13] H NAG
2-acetamido-2-deoxy-beta-D-glucopyranose[14 atoms]..
A 100.0
/99.4
2
/2
FURIN_HUMAN Furin
4hx2[1] I 1AX
(2R,2'R)-3,3'-oxydipropane-1,2-diol[11 atoms]
A 0.0
/49.2
2
/8
Q9FDF2_BACLI KerA
1scn[1] B 0EF
N-(tert-butoxycarbonyl)-L-alanyl-N-[(1R)-1-(carbox..
A 100.0
/49.2
1
/11
SUBT_BACLI SUBTILISIN CARLSBERG
1be8[2] C TCA
PHENYLETHYLENECARBOXYLIC ACID[10 atoms]
A 100.0
/49.2
1
/8
SUBT_BACLI SUBTILISIN CARLSBERG
1sue[2] C DFP
DIISOPROPYL PHOSPHONATE[7 atoms]
A 100.0
/47.1
1
/8
SUBT_BACAM SUBTILISIN BPN'
2id4[1] K MLA
MALONIC ACID[7 atoms]
A 75.0
/42.3
4
/4
KEX2_YEAST Kexin
1r64[1] V BTB
2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PR..
B 0.0
/42.2
5
/5
KEX2_YEAST Kexin
1y3c[4] K 15P
POLYETHYLENE GLYCOL (N=34)[12 atoms]
A 100.0
/40.9
2
/4
SUBT_BACAM subtilisin BPN'
1to2[16] I 15P
POLYETHYLENE GLYCOL (N=34)[15 atoms]
A 28.6
/40.9
7
/7
SUBT_BACAM Subtilisin BPN'
1y3d[2] K 15P
POLYETHYLENE GLYCOL (N=34)[17 atoms]
A 0.0
/40.9
1
/2
SUBT_BACAM subtilisin BPN'
1y48[15] H 15P
POLYETHYLENE GLYCOL (N=34)[11 atoms]
A 50.0
/40.9
4
/4
SUBT_BACAM subtilisin BPN'
5aqe[1] B VOD
(4-VINYLPHENYL)METHANESULFONIC ACID[12 atoms]
A 84.6
/37.0
13
/13
SUBS_BACLE SUBTILISIN SAVINASE
5arb[2] F EI3
5-methyl-2-(5-methylpyridin-2-yl)pyridine[14 atoms..
A 33.3
/37.0
3
/4
SUBS_BACLE SUBTILISIN SAVINASE
5arc[1] C EI3
5-methyl-2-(5-methylpyridin-2-yl)pyridine[14 atoms..
A 25.0
/37.0
4
/4
SUBS_BACLE SUBTILISIN SAVINASE
1sh7[4] F PMS
phenylmethanesulfonic acid[10 atoms]
A 75.0
/30.2
4
/7
Q8GB52_9VIBR extracellular subtilisin-like serine proteinase
1sup[1] D PMS
phenylmethanesulfonic acid[10 atoms]
A 100.0
/40.9
1
/9
SUBT_BACAM SUBTILISIN BPN'
3.a3:asym_id for the contact molecule. 4.a4:asym_id for the template homologue. 5.identity[%]5:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon6:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.
METAL
794 pdb_id contact mol homologue
a3 description a4 identity[%]5 Ncon6 description
5jxh[15] J CL
CHLORIDE ION[1 atoms]
A 100.0
/99.4
3
/3
FURIN_HUMAN Furin
3bx1[6] W CL
CHLORIDE ION[1 atoms]
B 0.0
/37.0
1
/3
SUBS_BACLE Subtilisin Savinase
3bx1[2] M CL
CHLORIDE ION[1 atoms]
A 16.7
/37.0
6
/6
SUBS_BACLE Subtilisin Savinase
3bx1[2] K CL
CHLORIDE ION[1 atoms]
A 0.0
/37.0
1
/1
SUBS_BACLE Subtilisin Savinase
3bx1[2] IA CL
CHLORIDE ION[1 atoms]
A 0.0
/37.0
1
/1
SUBS_BACLE Subtilisin Savinase
3bx1[2] F CL
CHLORIDE ION[1 atoms]
A 50.0
/37.0
2
/3
SUBS_BACLE Subtilisin Savinase
3bx1[2] O CL
CHLORIDE ION[1 atoms]
A 0.0
/37.0
1
/1
SUBS_BACLE Subtilisin Savinase
5arb[3] G CL
CHLORIDE ION[1 atoms]
A 25.0
/37.0
4
/4
SUBS_BACLE SUBTILISIN SAVINASE
3bx1[2] Z CL
CHLORIDE ION[1 atoms]
B 100.0
/37.0
4
/4
SUBS_BACLE Subtilisin Savinase
3bx1[3] X CL
CHLORIDE ION[1 atoms]
B 100.0
/37.0
1
/3
SUBS_BACLE Subtilisin Savinase
3bx1[4] L CL
CHLORIDE ION[1 atoms]
A 33.3
/37.0
3
/3
SUBS_BACLE Subtilisin Savinase
3bx1[2] H CL
CHLORIDE ION[1 atoms]
A 100.0
/37.0
2
/2
SUBS_BACLE Subtilisin Savinase
3bx1[2] J CL
CHLORIDE ION[1 atoms]
A 0.0
/37.0
2
/2
SUBS_BACLE Subtilisin Savinase
3ti9[1] F CL
CHLORIDE ION[1 atoms]
A 0.0
/35.7
1
/3
Q46547_DICNO Serine protease
2wuv[1] H CL
CHLORIDE ION[1 atoms]
A 66.7
/49.2
3
/3
SUBT_BACLI SUBTILISIN CARLSBERG
4hx2[1] H CL
CHLORIDE ION[1 atoms]
A 100.0
/49.2
1
/2
Q9FDF2_BACLI KerA
2wuv[2] I CS
CESIUM ION[1 atoms]
A 50.0
/49.2
4
/4
SUBT_BACLI SUBTILISIN CARLSBERG
4c3u[2] G CS
CESIUM ION[1 atoms]
A 0.0
/49.2
1
/2
SUBT_BACLI SUBTILISIN CARLSBERG
4c3u[2] K CS
CESIUM ION[1 atoms]
A 100.0
/49.2
1
/3
SUBT_BACLI SUBTILISIN CARLSBERG
4c3u[1] M CS
CESIUM ION[1 atoms]
A 50.0
/49.2
2
/2
SUBT_BACLI SUBTILISIN CARLSBERG
3co0[3] F ZN
ZINC ION[1 atoms]
B 0.0
/47.1
1
/1
SUBT_BACAM Subtilisin BPN'
3co0[3] E ZN
ZINC ION[1 atoms]
B 100.0
/47.1
3
/5
SUBT_BACAM Subtilisin BPN'
5jxh[15] H NA
SODIUM ION[1 atoms]
A 100.0
/99.4
3
/3
FURIN_HUMAN Furin
6hzd[15] G NA
SODIUM ION[1 atoms]
A 100.0
/99.4
2
/2
FURIN_HUMAN Furin
4omc[35] HB NA
SODIUM ION[1 atoms]
F 100.0
/100.0
4
/4
FURIN_HUMAN Furin
6y5s[9] C NA
SODIUM ION[1 atoms]
A 33.3
/37.0
6
/6
SUBS_BACLE Subtilisin Savinase
2wuw[2] C NA
SODIUM ION[1 atoms]
A 50.0
/49.2
4
/4
SUBT_BACLI SUBTILISIN CARLSBERG
3bx1[4] R NA
SODIUM ION[1 atoms]
A 50.0
/37.0
2
/2
SUBS_BACLE Subtilisin Savinase
5jxi[2] I NA
SODIUM ION[1 atoms]
A 100.0
/99.4
2
/2
FURIN_HUMAN Furin
6eqv[6] I NA
SODIUM ION[1 atoms]
A 100.0
/99.4
1
/1
FURIN_HUMAN Furin
1av7[3] C NA
SODIUM ION[1 atoms]
A 60.0
/49.2
5
/6
SUBT_BACLI SUBTILISIN CARLSBERG, TYPE VIII
3bx1[2] Q NA
SODIUM ION[1 atoms]
A 0.0
/37.0
2
/2
SUBS_BACLE Subtilisin Savinase
5jxi[5] F NA
SODIUM ION[1 atoms]
A 100.0
/99.4
4
/4
FURIN_HUMAN Furin
6f9m[2] D NA
SODIUM ION[1 atoms]
A 20.0
/38.2
5
/5
Serine protease
5jxi[2] G NA
SODIUM ION[1 atoms]
A 100.0
/99.4
3
/3
FURIN_HUMAN Furin
2id4[2] J NA
SODIUM ION[1 atoms]
A 60.0
/42.3
5
/5
KEX2_YEAST Kexin
5jxg[1] L NA
SODIUM ION[1 atoms]
A 100.0
/99.4
1
/1
FURIN_HUMAN Furin
1r64[2] M K
POTASSIUM ION[1 atoms]
A 0.0
/42.2
3
/3
KEX2_YEAST Kexin
1r64[2] S K
POTASSIUM ION[1 atoms]
B 33.3
/42.2
3
/4
KEX2_YEAST Kexin
1r64[1] U K
POTASSIUM ION[1 atoms]
B 0.0
/42.2
1
/1
KEX2_YEAST Kexin
1r64[1] N K
POTASSIUM ION[1 atoms]
A 100.0
/42.2
1
/1
KEX2_YEAST Kexin
4omc[40] FB CA
CALCIUM ION[1 atoms]
F 100.0
/100.0
3
/3
FURIN_HUMAN Furin
3ti7[174] D CA
CALCIUM ION[1 atoms]
A 66.7
/37.0
3
/5
A5EVD0_DICNV Basic extracellular subtilisin-like protease BprV
1r64[4] J CA
CALCIUM ION[1 atoms]
A 66.7
/42.2
6
/6
KEX2_YEAST Kexin
3hjr[2] C CA
CALCIUM ION[1 atoms]
A 50.0
/31.3
4
/6
Q9L5A4_AERSO Extracellular serine protease
4ryd[43] DA CA
CALCIUM ION[1 atoms]
C 100.0
/100.0
6
/6
FURIN_HUMAN Furin
5yl7[1] F CA
CALCIUM ION[1 atoms]
A 0.0
/31.1
3
/3
Pseudoalteromonas arctica PAMC 21717
1sca[4] D CA
CALCIUM ION[1 atoms]
A 50.0
/49.2
4
/4
SUBT_BACLI SUBTILISIN CARLSBERG
1r64[2] I CA
CALCIUM ION[1 atoms]
A 100.0
/42.2
3
/3
KEX2_YEAST Kexin
3tec[4] C CA
CALCIUM ION[1 atoms]
A 66.7
/44.7
6
/6
THET_THEVU THERMITASE
4tr2[2] J CA
CALCIUM ION[1 atoms]
B 60.0
/45.8
5
/6
E6Y8B9_PLAVI Subtilisin-like 1 serine protease
6o44[6] D CA
CALCIUM ION[1 atoms]
A 100.0
/41.8
1
/2
A0A024B5N4_BACIU Nattokinase
1ndq[13] C CA
CALCIUM ION[1 atoms]
A 25.0
/37.0
4
/4
SUBS_BACLE Subtilisin Savinase
1sh7[4] I CA
CALCIUM ION[1 atoms]
B 20.0
/30.2
5
/5
Q8GB52_9VIBR extracellular subtilisin-like serine proteinase
2id4[5] N CA
CALCIUM ION[1 atoms]
B 66.7
/42.3
6
/6
KEX2_YEAST Kexin
3hjr[2] B CA
CALCIUM ION[1 atoms]
A 50.0
/31.3
6
/6
Q9L5A4_AERSO Extracellular serine protease
1p8j[1] QC CA
CALCIUM ION[1 atoms]
G 100.0
/97.9
2
/2
FURI_MOUSE Furin precursor
1r64[4] K CA
CALCIUM ION[1 atoms]
A 60.0
/42.2
5
/5
KEX2_YEAST Kexin
4z2a[1] E CA
CALCIUM ION[1 atoms]
A 100.0
/99.6
3
/3
FURIN_HUMAN Furin
4lvn[2] F CA
CALCIUM ION[1 atoms]
A 40.0
/26.9
5
/6
Q868D6_PLAFA Subtilisin-like serine protease
3wqb[2] E CA
CALCIUM ION[1 atoms]
A 66.7
/31.0
3
/6
Q9L5A4_AERSO Extracellular serine protease
3lpa[3] C CA
CALCIUM ION[1 atoms]
A 66.7
/32.6
6
/6
A5EXI3_DICNV Acidic extracellular subtilisin-like protease AprV..
1ot5[2] L CA
CALCIUM ION[1 atoms]
B 100.0
/42.2
3
/3
KEX2_YEAST Kexin
3whi[3] D CA
CALCIUM ION[1 atoms]
B 50.0
/35.7
6
/6
SUBT_BACSU Subtilisin E
1p8j[1] QC CA
CALCIUM ION[1 atoms]
A 100.0
/97.9
1
/1
FURI_MOUSE Furin precursor
2id4[2] H CA
CALCIUM ION[1 atoms]
A 100.0
/42.3
3
/3
KEX2_YEAST Kexin
4z2a[1] D CA
CALCIUM ION[1 atoms]
A 100.0
/99.6
4
/4
FURIN_HUMAN Furin
2b6n[1] C CA
CALCIUM ION[1 atoms]
A 20.0
/29.7
5
/5
Q3HUQ2_9ENTR proteinase K
1dbi[1] B CA
CALCIUM ION[1 atoms]
A 40.0
/45.1
5
/6
THES_BACSJ AK.1 SERINE PROTEASE
1dbi[1] E CA
CALCIUM ION[1 atoms]
A 33.3
/45.1
3
/3
THES_BACSJ AK.1 SERINE PROTEASE
3.a3:asym_id for the contact molecule. 4.a4:asym_id for the template homologue. 5.identity[%]5:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon6:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.
OTHERPOLY
794 pdb_id contact mol homologue
a3 description a4 identity[%]5 Ncon6 description
1p8j[1] Q beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-b.. G 91.7
/97.9
12
/12
FURI_MOUSE Furin precursor
1p8j[1] Q beta-D-galactopyranose-(1-4)-2-acetamido-2-deoxy-b.. A 100.0
/97.9
1
/1
FURI_MOUSE Furin precursor
2id4[1] E 2-acetamido-2-deoxy-alpha-D-glucopyranose-(1-4)-2-.. A 0.0
/42.3
3
/3
KEX2_YEAST Kexin
1r64[1] E 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-a.. A 0.0
/42.2
4
/4
KEX2_YEAST Kexin
1ot5[1] E 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-a.. A 0.0
/42.2
4
/4
KEX2_YEAST Kexin
3.a3:asym_id for the contact molecule. 4.a4:asym_id for the template homologue. 5.identity[%]5:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon6:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.
HOMO
794 pdb_id contact mol homologue
a3 description a4 identity[%]5 Ncon6 description
1p8j[12] A FURI_MOUSE Furin precursor[470 aa] C 100.0
/97.9
5
/5
FURI_MOUSE Furin precursor
1p8j[8] A FURI_MOUSE Furin precursor[470 aa] B 92.6
/97.9
27
/27
FURI_MOUSE Furin precursor
1p8j[4] B FURI_MOUSE Furin precursor[468 aa] C 100.0
/97.9
6
/6
FURI_MOUSE Furin precursor
1p8j[1] A FURI_MOUSE Furin precursor[470 aa] G 90.9
/97.9
11
/11
FURI_MOUSE Furin precursor
1p8j[1] G FURI_MOUSE Furin precursor[467 aa] A 100.0
/97.9
11
/11
FURI_MOUSE Furin precursor
3qtl[1] A Q1EM64_BACLI Subtilisin-like serin protease[269 aa] B 0.0
/49.2
2
/2
Q1EM64_BACLI Subtilisin-like serin protease
3qtl[1] A Q1EM64_BACLI Subtilisin-like serin protease[269 aa] C 0.0
/49.2
3
/7
Q1EM64_BACLI Subtilisin-like serin protease
4tr2[1] A E6Y8B9_PLAVI Subtilisin-like 1 serine protease[471 aa] B 50.0
/45.8
2
/39
E6Y8B9_PLAVI Subtilisin-like 1 serine protease
4tr2[1] B E6Y8B9_PLAVI Subtilisin-like 1 serine protease[474 aa] A 50.0
/45.8
2
/42
E6Y8B9_PLAVI Subtilisin-like 1 serine protease
1y48[16] A SUBT_BACAM subtilisin BPN' [281 aa] A 100.0
/40.9
1
/6
SUBT_BACAM subtilisin BPN'
1tm5[8] A SUBT_BACAM Subtilisin BPN' [281 aa] A 66.7
/40.9
6
/9
SUBT_BACAM Subtilisin BPN'
3bx1[2] A SUBS_BACLE Subtilisin Savinase[269 aa] A 27.3
/37.0
11
/11
SUBS_BACLE Subtilisin Savinase
3whi[2] A SUBT_BACSU Subtilisin E[355 aa] A 14.3
/36.6
7
/12
SUBT_BACSU Subtilisin E
3.a3:asym_id for the contact molecule. 4.a4:asym_id for the template homologue. 5.identity[%]5:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon6:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.
PRECIPITANT
794 pdb_id contact mol homologue
a3 description a4 identity[%]5 Ncon6 description
4omd[36] S FMT
FORMIC ACID[3 atoms]
B 100.0
/100.0
4
/4
FURIN_HUMAN Furin
4omc[12] M FMT
FORMIC ACID[3 atoms]
A 100.0
/100.0
4
/4
FURIN_HUMAN Furin
1c3l[1] G FMT
FORMIC ACID[3 atoms]
A 100.0
/49.2
1
/3
SUBT_BACLI SUBTILISIN-CARLSBERG
4omc[6] NA FMT
FORMIC ACID[3 atoms]
D 100.0
/100.0
5
/5
FURIN_HUMAN Furin
1c3l[1] E FMT
FORMIC ACID[3 atoms]
A 100.0
/49.2
1
/6
SUBT_BACLI SUBTILISIN-CARLSBERG
6dwq[1] N EDO
1,2-ETHANEDIOL[4 atoms]
A 0.0
/49.2
2
/2
Q9FDF2_BACLI KerA
6dwq[1] D EDO
1,2-ETHANEDIOL[4 atoms]
A 50.0
/49.2
2
/4
Q9FDF2_BACLI KerA
6dwq[1] M EDO
1,2-ETHANEDIOL[4 atoms]
A 66.7
/49.2
3
/4
Q9FDF2_BACLI KerA
6dwq[1] E EDO
1,2-ETHANEDIOL[4 atoms]
A 0.0
/49.2
4
/6
Q9FDF2_BACLI KerA
6dwq[1] L EDO
1,2-ETHANEDIOL[4 atoms]
A 33.3
/49.2
3
/5
Q9FDF2_BACLI KerA
6o44[1] F EDO
1,2-ETHANEDIOL[4 atoms]
A 100.0
/41.8
1
/3
A0A024B5N4_BACIU Nattokinase
4z2a[1] H EDO
1,2-ETHANEDIOL[4 atoms]
A 100.0
/99.6
5
/5
FURIN_HUMAN Furin
6hld[7] K PO4
PHOSPHATE ION[5 atoms]
A 100.0
/99.4
2
/2
FURIN_HUMAN Furin
6hld[7] J PO4
PHOSPHATE ION[5 atoms]
A 100.0
/99.4
4
/4
FURIN_HUMAN Furin
4tr2[1] H PO4
PHOSPHATE ION[5 atoms]
A 33.3
/45.8
3
/6
E6Y8B9_PLAVI Subtilisin-like 1 serine protease
4z2a[2] F PO4
PHOSPHATE ION[5 atoms]
A 100.0
/99.6
6
/6
FURIN_HUMAN Furin
6hld[7] L DMS
DIMETHYL SULFOXIDE[4 atoms]
A 100.0
/99.4
6
/6
FURIN_HUMAN Furin
1wsd[1] C SO4
SULFATE ION[5 atoms]
A 50.0
/37.0
2
/3
PRTM_BACSK M-protease
1p8j[10] ZA SO4
SULFATE ION[5 atoms]
C 100.0
/97.9
1
/1
FURI_MOUSE Furin precursor
1p8j[1] MA SO4
SULFATE ION[5 atoms]
B 100.0
/97.9
3
/3
FURI_MOUSE Furin precursor
4cfz[10] I SO4
SULFATE ION[5 atoms]
A 100.0
/37.0
1
/2
SUBS_BACLE SUBTILISIN SAVINASE
1p8j[9] ZC SO4
SULFATE ION[5 atoms]
G 100.0
/97.9
3
/3
FURI_MOUSE Furin precursor
4cfz[1] D SO4
SULFATE ION[5 atoms]
A 0.0
/37.0
2
/2
SUBS_BACLE SUBTILISIN SAVINASE
1p8j[15] YC SO4
SULFATE ION[5 atoms]
G 100.0
/97.9
1
/1
FURI_MOUSE Furin precursor
1p8j[7] AC SO4
SULFATE ION[5 atoms]
G 100.0
/97.9
1
/1
FURI_MOUSE Furin precursor
1p8j[2] TB SO4
SULFATE ION[5 atoms]
E 100.0
/97.9
3
/3
FURI_MOUSE Furin precursor
4cfz[6] F SO4
SULFATE ION[5 atoms]
A 0.0
/37.0
3
/3
SUBS_BACLE SUBTILISIN SAVINASE
1p8j[5] GC SO4
SULFATE ION[5 atoms]
G 100.0
/97.9
2
/2
FURI_MOUSE Furin precursor
1p8j[4] ZA SO4
SULFATE ION[5 atoms]
D 100.0
/97.9
1
/1
FURI_MOUSE Furin precursor
4cfz[10] H SO4
SULFATE ION[5 atoms]
A 50.0
/37.0
4
/4
SUBS_BACLE SUBTILISIN SAVINASE
1p8j[2] X SO4
SULFATE ION[5 atoms]
C 100.0
/97.9
4
/4
FURI_MOUSE Furin precursor
4cfz[1] E SO4
SULFATE ION[5 atoms]
A 0.0
/37.0
2
/4
SUBS_BACLE SUBTILISIN SAVINASE
1p8j[1] EA SO4
SULFATE ION[5 atoms]
A 100.0
/97.9
3
/3
FURI_MOUSE Furin precursor
1p8j[2] JC SO4
SULFATE ION[5 atoms]
G 100.0
/97.9
5
/5
FURI_MOUSE Furin precursor
1p8j[4] DA SO4
SULFATE ION[5 atoms]
A 100.0
/97.9
3
/3
FURI_MOUSE Furin precursor
1p8j[1] SC SO4
SULFATE ION[5 atoms]
H 100.0
/97.9
2
/2
FURI_MOUSE Furin precursor
1p8j[1] EC SO4
SULFATE ION[5 atoms]
F 50.0
/97.9
2
/2
FURI_MOUSE Furin precursor
1p8j[1] XC SO4
SULFATE ION[5 atoms]
H 100.0
/97.9
3
/3
FURI_MOUSE Furin precursor
2b6n[1] D SO4
SULFATE ION[5 atoms]
A 20.0
/29.7
5
/5
Q3HUQ2_9ENTR proteinase K
1p8j[1] WC SO4
SULFATE ION[5 atoms]
A 100.0
/97.9
1
/1
FURI_MOUSE Furin precursor
1p8j[1] BA SO4
SULFATE ION[5 atoms]
A 100.0
/97.9
1
/1
FURI_MOUSE Furin precursor
1p8j[1] UC SO4
SULFATE ION[5 atoms]
G 100.0
/97.9
6
/6
FURI_MOUSE Furin precursor
1p8j[1] VC SO4
SULFATE ION[5 atoms]
G 100.0
/97.9
3
/3
FURI_MOUSE Furin precursor
4c3v[1] C SO4
SULFATE ION[5 atoms]
A 50.0
/49.2
2
/3
SUBT_BACLI SUBTILISIN CARLSBERG
1p8j[1] SC SO4
SULFATE ION[5 atoms]
G 100.0
/97.9
3
/3
FURI_MOUSE Furin precursor
1af4[3] H DIO
1,4-DIETHYLENE DIOXIDE[6 atoms]
A 100.0
/49.2
2
/4
SUBT_BACLI SUBTILISIN CARLSBERG
1af4[1] E DIO
1,4-DIETHYLENE DIOXIDE[6 atoms]
A 100.0
/49.2
1
/4
SUBT_BACLI SUBTILISIN CARLSBERG
3lpc[1] H ACT
ACETATE ION[4 atoms]
A 0.0
/32.6
4
/4
AprB2
3lpc[1] F ACT
ACETATE ION[4 atoms]
A 100.0
/32.6
2
/2
AprB2
3lpc[1] G ACT
ACETATE ION[4 atoms]
A 0.0
/32.6
3
/3
AprB2
3lpc[1] E ACT
ACETATE ION[4 atoms]
A 100.0
/32.6
5
/6
AprB2
4hx2[1] S ACT
ACETATE ION[4 atoms]
C 0.0
/49.2
1
/5
Q9FDF2_BACLI KerA
4hx2[1] U IPA
ISOPROPYL ALCOHOL[4 atoms]
C 100.0
/49.2
2
/3
Q9FDF2_BACLI KerA
4hx2[1] L IPA
ISOPROPYL ALCOHOL[4 atoms]
A 66.7
/49.2
6
/6
Q9FDF2_BACLI KerA
1scb[4] M CCN
ACETONITRILE[3 atoms]
A 0.0
/49.2
2
/2
SUBT_BACLI SUBTILISIN CARLSBERG
1bfk[7] C CCN
ACETONITRILE[3 atoms]
A 100.0
/49.2
1
/3
SUBT_BACLI SUBTILISIN CARLSBERG
1bfk[2] G CCN
ACETONITRILE[3 atoms]
A 0.0
/49.2
5
/5
SUBT_BACLI SUBTILISIN CARLSBERG
1be6[3] G CCN
ACETONITRILE[3 atoms]
A 33.3
/49.2
3
/3
SUBT_BACLI SUBTILISIN CARLSBERG
1be6[1] E CCN
ACETONITRILE[3 atoms]
A 0.0
/49.2
2
/2
SUBT_BACLI SUBTILISIN CARLSBERG
3bgo[1] C AZI
AZIDE ION[3 atoms]
B 40.0
/47.1
5
/8
SUBT_BACAM Subtilisin BPN'
2sbt[1] B ACN
ACETONE[4 atoms]
A 37.5
/43.3
8
/8
SUBT_BACAM SUBTILISIN NOVO
1tmg[4] L 1PE
PENTAETHYLENE GLYCOL[9 atoms]
A 25.0
/40.9
4
/4
SUBT_BACAM Subtilisin BPN'
1tmg[21] H 1PE
PENTAETHYLENE GLYCOL[11 atoms]
A 50.0
/40.9
4
/4
SUBT_BACAM Subtilisin BPN'
1tm3[12] I 1PE
PENTAETHYLENE GLYCOL[13 atoms]
A 16.7
/40.9
6
/6
SUBT_BACAM Subtilisin BPN' precursor
1y48[16] E CIT
CITRIC ACID[13 atoms]
A 100.0
/40.9
1
/4
SUBT_BACAM subtilisin BPN'
1v5i[1] M GOL
GLYCEROL[6 atoms]
A 0.0
/40.9
1
/4
SUBT_BACAM Subtilisin BPN'
1v5i[2] L GOL
GLYCEROL[6 atoms]
A 66.7
/40.9
3
/3
SUBT_BACAM Subtilisin BPN'
1v5i[2] K GOL
GLYCEROL[6 atoms]
A 100.0
/40.9
2
/3
SUBT_BACAM Subtilisin BPN'
3unx[1] B GOL
GLYCEROL[6 atoms]
A 0.0
/49.2
2
/4
SUBT_BACLI Subtilisin Carlsberg
3vyv[1] D GOL
GLYCEROL[6 atoms]
A 75.0
/41.8
4
/4
SUBN_BACNA Subtilisin NAT
5aqe[2] F GOL
GLYCEROL[6 atoms]
A 100.0
/37.0
2
/4
SUBS_BACLE SUBTILISIN SAVINASE
1v5i[1] E GOL
GLYCEROL[6 atoms]
A 66.7
/40.9
3
/4
SUBT_BACAM Subtilisin BPN'
5ard[2] C GOL
GLYCEROL[6 atoms]
A 33.3
/37.0
6
/6
SUBS_BACLE SUBTILISIN SAVINASE
5arb[1] D GOL
GLYCEROL[6 atoms]
A 16.7
/37.0
6
/6
SUBS_BACLE SUBTILISIN SAVINASE
3ti9[1] E GOL
GLYCEROL[6 atoms]
A 12.5
/35.7
8
/8
Q46547_DICNO Serine protease
3lpc[1] I PEG
DI(HYDROXYETHYL)ETHER[7 atoms]
A 0.0
/32.6
4
/4
AprB2
3.a3:asym_id for the contact molecule. 4.a4:asym_id for the template homologue. 5.identity[%]5:sequence identity between the query and the template homologue only for the contact residues. Number after the slash / is sequence identity for all the aligned region. 6.Ncon6:number of aligned contact residues for the query. Number after the slash / is number of contact residues in the template homologue.