|
eF-site ID
|
1bt7_15-A |
PDB Code
|
1bt7 |
Model
|
15 |
Chain
|
A |
|
click to enlarge
|
|
Title
|
THE SOLUTION NMR STRUCTURE OF THE N-TERMINAL PROTEASE DOMAIN OF THE HEPATITIS C VIRUS (HCV) NS3-PROTEIN, FROM BK STRAIN, 20 STRUCTURES |
Classification
|
HYDROLASE |
Compound
|
NS3 SERINE PROTEASE |
Source
|
Hepatitis C virus genotype 1b (isolate BK) (HCV) (POLG_HCVBK) |
|
Sequence
|
A: |
TGRDKNQVEGEVQVVSTATQSFLATCVNGVCWTVYHGAGS
KTLAGPKGPITQMYTNVDQDLVGWQAPPGARSLTPCTCGS
SDLYLVTRHADVIPVRRRGDSRGSLLSPRPVSYLKGSSGG
PLLCPSGHAVGIFRAAVCTRGVAKAVDFVPVESMETTMRA
SKKKK
|
|
Description
|
|
Functional site
|
|
1)
|
chain |
A |
residue |
57 |
type |
|
sequence |
H
|
description |
CATALYTIC SITE
|
source |
: CTS
|
|
2)
|
chain |
A |
residue |
81 |
type |
|
sequence |
D
|
description |
CATALYTIC SITE
|
source |
: CTS
|
|
3)
|
chain |
A |
residue |
139 |
type |
|
sequence |
S
|
description |
CATALYTIC SITE
|
source |
: CTS
|
|
4)
|
chain |
A |
residue |
97 |
type |
|
sequence |
C
|
description |
ZINC BINDING SITE
|
source |
: ZNB
|
|
5)
|
chain |
A |
residue |
99 |
type |
|
sequence |
C
|
description |
ZINC BINDING SITE
|
source |
: ZNB
|
|
6)
|
chain |
A |
residue |
145 |
type |
|
sequence |
C
|
description |
ZINC BINDING SITE
|
source |
: ZNB
|
|
7)
|
chain |
A |
residue |
97 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 301
|
source |
: AC1
|
|
8)
|
chain |
A |
residue |
99 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 301
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
145 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE ZN A 301
|
source |
: AC1
|
|
10)
|
chain |
A |
residue |
151 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE ZN A 301
|
source |
: AC1
|
|
11)
|
chain |
A |
residue |
57 |
type |
ACT_SITE |
sequence |
H
|
description |
Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8861916
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
12)
|
chain |
A |
residue |
81 |
type |
ACT_SITE |
sequence |
D
|
description |
Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8861916
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
13)
|
chain |
A |
residue |
139 |
type |
ACT_SITE |
sequence |
S
|
description |
Charge relay system; for serine protease NS3 activity => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:8861916, ECO:0000269|PubMed:9568891
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
14)
|
chain |
A |
residue |
97 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:10366511, ECO:0000269|PubMed:8861916, ECO:0000269|PubMed:9568891
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
15)
|
chain |
A |
residue |
99 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:10366511, ECO:0000269|PubMed:8861916, ECO:0000269|PubMed:9568891
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
16)
|
chain |
A |
residue |
145 |
type |
BINDING |
sequence |
C
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:10366511, ECO:0000269|PubMed:8861916
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
17)
|
chain |
A |
residue |
149 |
type |
BINDING |
sequence |
H
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU01166, ECO:0000269|PubMed:10366511, ECO:0000269|PubMed:8861916
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
|
|