|
eF-site ID
|
1rgq-ABCD |
PDB Code
|
1rgq |
Chain
|
A, B, C, D |
|
click to enlarge
|
|
Title
|
M9A HCV Protease complex with pentapeptide keto-amide inhibitor |
Classification
|
Viral protein, hydrolase |
Compound
|
NS3 Protease |
Source
|
Hepatitis C virus genotype 1a (isolate H) (HCV) (O39914_9HEPC) |
|
Sequence
|
A: |
QVEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASP
KGPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLV
TRHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPA
GHAVGLFRAAVCTRGVTKAVDFIPVENLETTMRS
|
B: |
QMGAPITAYAQQTRGLLGCIITSLTGRDKNQVEGEVQIVS
TATQTFLATCINGVCWTVYHGAGTRTIASPKGPVIQMYTN
VDQDLVGWPAPQGSRSLTPCTCGSSDLYLVTRHADVIPVR
RRGDSRGSLLSPRPISYLKGSSGGPLLCPAGHAVGLFRAA
VCTRGVTKAVDFIPVENLETTMRSGS
|
C: |
KGSVVIVGRIVLSGKPAIIPKK
|
D: |
GSVVIVGRIVLSGKPAI
|
|
Description
|
(1) |
NS3 Protease (E.C.3.4.21.98), NS4A peptide
|
|
Functional site
|
|
1)
|
chain |
A |
residue |
100 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 193
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
101 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE ZN A 193
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
102 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 193
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
148 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 193
|
source |
: AC1
|
|
5)
|
chain |
B |
residue |
100 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 193
|
source |
: AC2
|
|
6)
|
chain |
B |
residue |
102 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 193
|
source |
: AC2
|
|
7)
|
chain |
B |
residue |
148 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN B 193
|
source |
: AC2
|
|
8)
|
chain |
B |
residue |
44 |
type |
|
sequence |
Q
|
description |
BINDING SITE FOR RESIDUE AKP B 194
|
source |
: AC3
|
|
9)
|
chain |
B |
residue |
45 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE AKP B 194
|
source |
: AC3
|
|
10)
|
chain |
B |
residue |
60 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE AKP B 194
|
source |
: AC3
|
|
11)
|
chain |
B |
residue |
135 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE AKP B 194
|
source |
: AC3
|
|
12)
|
chain |
B |
residue |
138 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE AKP B 194
|
source |
: AC3
|
|
13)
|
chain |
B |
residue |
139 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE AKP B 194
|
source |
: AC3
|
|
14)
|
chain |
B |
residue |
140 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE AKP B 194
|
source |
: AC3
|
|
15)
|
chain |
B |
residue |
141 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE AKP B 194
|
source |
: AC3
|
|
16)
|
chain |
B |
residue |
142 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE AKP B 194
|
source |
: AC3
|
|
17)
|
chain |
B |
residue |
158 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE AKP B 194
|
source |
: AC3
|
|
18)
|
chain |
B |
residue |
159 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE AKP B 194
|
source |
: AC3
|
|
19)
|
chain |
B |
residue |
160 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE AKP B 194
|
source |
: AC3
|
|
20)
|
chain |
B |
residue |
161 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE AKP B 194
|
source |
: AC3
|
|
21)
|
chain |
B |
residue |
162 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE AKP B 194
|
source |
: AC3
|
|
22)
|
chain |
A |
residue |
61 |
type |
catalytic |
sequence |
G
|
description |
776
|
source |
MCSA : MCSA1
|
|
23)
|
chain |
A |
residue |
85 |
type |
catalytic |
sequence |
L
|
description |
776
|
source |
MCSA : MCSA1
|
|
24)
|
chain |
A |
residue |
141 |
type |
catalytic |
sequence |
S
|
description |
776
|
source |
MCSA : MCSA1
|
|
25)
|
chain |
A |
residue |
143 |
type |
catalytic |
sequence |
G
|
description |
776
|
source |
MCSA : MCSA1
|
|
26)
|
chain |
B |
residue |
61 |
type |
catalytic |
sequence |
G
|
description |
776
|
source |
MCSA : MCSA2
|
|
27)
|
chain |
B |
residue |
85 |
type |
catalytic |
sequence |
L
|
description |
776
|
source |
MCSA : MCSA2
|
|
28)
|
chain |
B |
residue |
141 |
type |
catalytic |
sequence |
S
|
description |
776
|
source |
MCSA : MCSA2
|
|
29)
|
chain |
B |
residue |
143 |
type |
catalytic |
sequence |
G
|
description |
776
|
source |
MCSA : MCSA2
|
|
30)
|
chain |
A |
residue |
61 |
type |
ACT_SITE |
sequence |
G
|
description |
Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8386278, ECO:0000305|PubMed:8861917
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
31)
|
chain |
B |
residue |
61 |
type |
ACT_SITE |
sequence |
G
|
description |
Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8386278, ECO:0000305|PubMed:8861917
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
32)
|
chain |
A |
residue |
85 |
type |
ACT_SITE |
sequence |
L
|
description |
Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000305|PubMed:8861917
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
33)
|
chain |
B |
residue |
85 |
type |
ACT_SITE |
sequence |
L
|
description |
Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000305|PubMed:8861917
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
34)
|
chain |
A |
residue |
143 |
type |
ACT_SITE |
sequence |
G
|
description |
Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8248148, ECO:0000269|PubMed:8386278, ECO:0000305|PubMed:8861917
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
35)
|
chain |
B |
residue |
143 |
type |
ACT_SITE |
sequence |
G
|
description |
Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8248148, ECO:0000269|PubMed:8386278, ECO:0000305|PubMed:8861917
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
36)
|
chain |
A |
residue |
101 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982, ECO:0007744|PDB:1A1R, ECO:0007744|PDB:1N1L, ECO:0007744|PDB:1RGQ, ECO:0007744|PDB:2A4R, ECO:0007744|PDB:2F9V, ECO:0007744|PDB:2O8M, ECO:0007744|PDB:2OBQ, ECO:0007744|PDB:2OC0, ECO:0007744|PDB:2OC1, ECO:0007744|PDB:2OC7, ECO:0007744|PDB:2OC8, ECO:0007744|PDB:2OIN, ECO:0007744|PDB:2XNI
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
37)
|
chain |
A |
residue |
103 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982, ECO:0007744|PDB:1A1R, ECO:0007744|PDB:1N1L, ECO:0007744|PDB:1RGQ, ECO:0007744|PDB:2A4R, ECO:0007744|PDB:2F9V, ECO:0007744|PDB:2O8M, ECO:0007744|PDB:2OBQ, ECO:0007744|PDB:2OC0, ECO:0007744|PDB:2OC1, ECO:0007744|PDB:2OC7, ECO:0007744|PDB:2OC8, ECO:0007744|PDB:2OIN, ECO:0007744|PDB:2XNI
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
38)
|
chain |
B |
residue |
101 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982, ECO:0007744|PDB:1A1R, ECO:0007744|PDB:1N1L, ECO:0007744|PDB:1RGQ, ECO:0007744|PDB:2A4R, ECO:0007744|PDB:2F9V, ECO:0007744|PDB:2O8M, ECO:0007744|PDB:2OBQ, ECO:0007744|PDB:2OC0, ECO:0007744|PDB:2OC1, ECO:0007744|PDB:2OC7, ECO:0007744|PDB:2OC8, ECO:0007744|PDB:2OIN, ECO:0007744|PDB:2XNI
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
39)
|
chain |
B |
residue |
103 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982, ECO:0007744|PDB:1A1R, ECO:0007744|PDB:1N1L, ECO:0007744|PDB:1RGQ, ECO:0007744|PDB:2A4R, ECO:0007744|PDB:2F9V, ECO:0007744|PDB:2O8M, ECO:0007744|PDB:2OBQ, ECO:0007744|PDB:2OC0, ECO:0007744|PDB:2OC1, ECO:0007744|PDB:2OC7, ECO:0007744|PDB:2OC8, ECO:0007744|PDB:2OIN, ECO:0007744|PDB:2XNI
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
40)
|
chain |
A |
residue |
149 |
type |
BINDING |
sequence |
P
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982, ECO:0007744|PDB:1N1L, ECO:0007744|PDB:1RGQ, ECO:0007744|PDB:2A4R, ECO:0007744|PDB:2F9V, ECO:0007744|PDB:2O8M, ECO:0007744|PDB:2OBQ, ECO:0007744|PDB:2OC0, ECO:0007744|PDB:2OC1, ECO:0007744|PDB:2OC7, ECO:0007744|PDB:2OC8, ECO:0007744|PDB:2OIN, ECO:0007744|PDB:2XNI
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
41)
|
chain |
B |
residue |
149 |
type |
BINDING |
sequence |
P
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982, ECO:0007744|PDB:1N1L, ECO:0007744|PDB:1RGQ, ECO:0007744|PDB:2A4R, ECO:0007744|PDB:2F9V, ECO:0007744|PDB:2O8M, ECO:0007744|PDB:2OBQ, ECO:0007744|PDB:2OC0, ECO:0007744|PDB:2OC1, ECO:0007744|PDB:2OC7, ECO:0007744|PDB:2OC8, ECO:0007744|PDB:2OIN, ECO:0007744|PDB:2XNI
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
42)
|
chain |
A |
residue |
153 |
type |
BINDING |
sequence |
A
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
43)
|
chain |
B |
residue |
153 |
type |
BINDING |
sequence |
A
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
44)
|
chain |
B |
residue |
4 |
type |
SITE |
sequence |
A
|
description |
Cleavage; by protease NS2 => ECO:0000255|PROSITE-ProRule:PRU01030
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
|
|