|
eF-site ID
|
2oc1-C |
PDB Code
|
2oc1 |
Chain
|
C |
|
click to enlarge
|
|
Title
|
Structure of the HCV NS3/4A Protease Inhibitor CVS4819 |
Classification
|
VIRAL PROTEIN |
Compound
|
Hepatitis C virus |
Source
|
Hepatitis C virus subtype 1a (Q9QP06_9HEPC) |
|
Sequence
|
C: |
VEGEVQIVSTATQTFLATCINGVCWTVYHGAGTRTIASPK
GPVIQMYTNVDQDLVGWPAPQGSRSLTPCTCGSSDLYLVT
RHADVIPVRRRGDSRGSLLSPRPISYLKGSSGGPLLCPAG
HAVGLFRAAVCTRGVAKAVDFIPVENLETTM
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
C |
residue |
97 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN C 902
|
source |
: AC2
|
|
2)
|
chain |
C |
residue |
99 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN C 902
|
source |
: AC2
|
|
3)
|
chain |
C |
residue |
145 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN C 902
|
source |
: AC2
|
|
4)
|
chain |
C |
residue |
57 |
type |
catalytic |
sequence |
H
|
description |
776
|
source |
MCSA : MCSA2
|
|
5)
|
chain |
C |
residue |
81 |
type |
catalytic |
sequence |
D
|
description |
776
|
source |
MCSA : MCSA2
|
|
6)
|
chain |
C |
residue |
137 |
type |
catalytic |
sequence |
G
|
description |
776
|
source |
MCSA : MCSA2
|
|
7)
|
chain |
C |
residue |
139 |
type |
catalytic |
sequence |
S
|
description |
776
|
source |
MCSA : MCSA2
|
|
8)
|
chain |
C |
residue |
57 |
type |
ACT_SITE |
sequence |
H
|
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
|
|
9)
|
chain |
C |
residue |
81 |
type |
ACT_SITE |
sequence |
D
|
description |
Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000305|PubMed:8861917
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
10)
|
chain |
C |
residue |
139 |
type |
ACT_SITE |
sequence |
S
|
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
|
|
11)
|
chain |
C |
residue |
97 |
type |
BINDING |
sequence |
C
|
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
|
|
12)
|
chain |
C |
residue |
99 |
type |
BINDING |
sequence |
C
|
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
|
|
13)
|
chain |
C |
residue |
145 |
type |
BINDING |
sequence |
C
|
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
|
|
14)
|
chain |
C |
residue |
149 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:21507982
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
|
|