eF-site ID 6eqx-AD
PDB Code 6eqx
Chain A, D

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Title X-ray structure of the proprotein convertase furin bound with the competitive inhibitor Arg-Arg-Arg-Val-Arg-Amba
Classification HYDROLASE
Compound Furin
Source Homo sapiens (Human) (6EQX)
Sequence A:  VYQEPTDPKFPQQWYLSGVTQRDLNVKAAWAQGYTGHGIV
VSILDDGIEKNHPDLAGNYDPGASFDVNDQDPDPQPRYTQ
MNDNRHGTRCAGEVAAVANNGVCGVGVAYNARIGGVRMLD
GEVTDAVEARSLGLNPNHIHIYSASWGPEDDGKTVDGPAR
LAEEAFFRGVSQGRGGLGSIFVWASGNGGREHDSCNCDGY
TNSIYTLSISSATQFGNVPWYSEACSSTLATTYSSGNQNE
KQIVTTDLRQKCTESHTGTSASAPLAAGIIALTLEANKNL
TWRDMQHLVVQTSKPAHLNANDWATNGVGRKVSHSYGYGL
LDAGAMVALAQNWTTVAPQRKCIIDILTEPKDIGKRLEVR
KTVTACLGEPNHITRLEHAQARLTLSYNRRGDLAIHLVSP
MGTRSTLLAARPHDYSADGFNDWAFMTTHSWDEDPSGEWV
LEIENTSEANNYGTLTKFTLVLYGTASGSLVPR
D:  RRRVRX
Description


Functional site
1) chain A
residue 174
type
sequence D
description binding site for residue CA A 601
source : AC1
2) chain A
residue 179
type
sequence D
description binding site for residue CA A 601
source : AC1
3) chain A
residue 181
type
sequence D
description binding site for residue CA A 601
source : AC1
4) chain A
residue 115
type
sequence D
description binding site for residue CA A 602
source : AC2
5) chain A
residue 162
type
sequence D
description binding site for residue CA A 602
source : AC2
6) chain A
residue 205
type
sequence V
description binding site for residue CA A 602
source : AC2
7) chain A
residue 208
type
sequence N
description binding site for residue CA A 602
source : AC2
8) chain A
residue 210
type
sequence V
description binding site for residue CA A 602
source : AC2
9) chain A
residue 212
type
sequence G
description binding site for residue CA A 602
source : AC2
10) chain A
residue 258
type
sequence D
description binding site for residue CA A 603
source : AC3
11) chain A
residue 301
type
sequence D
description binding site for residue CA A 603
source : AC3
12) chain A
residue 331
type
sequence E
description binding site for residue CA A 603
source : AC3
13) chain A
residue 309
type
sequence T
description binding site for residue NA A 604
source : AC4
14) chain A
residue 311
type
sequence S
description binding site for residue NA A 604
source : AC4
15) chain A
residue 314
type
sequence T
description binding site for residue NA A 604
source : AC4
16) chain A
residue 279
type
sequence S
description binding site for residue NA A 605
source : AC5
17) chain A
residue 284
type
sequence G
description binding site for residue NA A 605
source : AC5
18) chain A
residue 544
type
sequence S
description binding site for residue NA A 606
source : AC6
19) chain A
residue 544
type
sequence S
description binding site for residue NA A 606
source : AC6
20) chain A
residue 546
type
sequence E
description binding site for residue NA A 607
source : AC7
21) chain A
residue 546
type
sequence E
description binding site for residue NA A 607
source : AC7
22) chain A
residue 313
type
sequence Y
description binding site for residue CL A 608
source : AC8
23) chain A
residue 449
type
sequence K
description binding site for residue CL A 608
source : AC8
24) chain A
residue 571
type
sequence Y
description binding site for residue CL A 608
source : AC8
25) chain A
residue 149-160
type prosite
sequence VSILDDGIEKNH
description SUBTILASE_ASP Serine proteases, subtilase family, aspartic acid active site. VSILDDGIeknH
source prosite : PS00136
26) chain A
residue 194-204
type prosite
sequence HGTRCAGEVAA
description SUBTILASE_HIS Serine proteases, subtilase family, histidine active site. HGTrCAGeVAA
source prosite : PS00137
27) chain A
residue 366-376
type prosite
sequence GTSASAPLAAG
description SUBTILASE_SER Serine proteases, subtilase family, serine active site. GTSaSaPlAAG
source prosite : PS00138
28) chain A
residue 194
type ACT_SITE
sequence H
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
source Swiss-Prot : SWS_FT_FI1
29) chain A
residue 368
type ACT_SITE
sequence S
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
source Swiss-Prot : SWS_FT_FI1
30) chain A
residue 153
type ACT_SITE
sequence D
description Charge relay system => ECO:0000255|PROSITE-ProRule:PRU01240
source Swiss-Prot : SWS_FT_FI1
31) chain A
residue 258
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI2
32) chain A
residue 301
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI2
33) chain A
residue 331
type BINDING
sequence E
description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI2
34) chain A
residue 179
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI2
35) chain A
residue 181
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI2
36) chain A
residue 205
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI2
37) chain A
residue 208
type BINDING
sequence N
description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI2
38) chain A
residue 210
type BINDING
sequence V
description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI2
39) chain A
residue 212
type BINDING
sequence G
description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI2
40) chain A
residue 162
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI2
41) chain A
residue 174
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI2
42) chain A
residue 115
type BINDING
sequence D
description BINDING => ECO:0000269|PubMed:24666235, ECO:0000269|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI2
43) chain A
residue 236
type BINDING
sequence E
description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI3
44) chain A
residue 253
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI3
45) chain A
residue 264
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI3
46) chain A
residue 292
type BINDING
sequence A
description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI3
47) chain A
residue 306
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI3
48) chain A
residue 308
type BINDING
sequence Y
description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI3
49) chain A
residue 368
type BINDING
sequence S
description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI3
50) chain A
residue 191
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI3
51) chain A
residue 154
type BINDING
sequence D
description BINDING => ECO:0000305|PubMed:24666235, ECO:0000305|PubMed:25974265, ECO:0007744|PDB:4OMC, ECO:0007744|PDB:4OMD, ECO:0007744|PDB:4RYD
source Swiss-Prot : SWS_FT_FI3
52) chain A
residue 440
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI4
53) chain A
residue 553
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI4
54) chain A
residue 387
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI4

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