|
|
1)
|
chain |
A |
residue |
9 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00541
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
2)
|
chain |
A |
residue |
15 |
type |
SITE |
sequence |
K
|
description |
Substrate binding => ECO:0000269|PubMed:18004778
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
3)
|
chain |
A |
residue |
273 |
type |
SITE |
sequence |
R
|
description |
Substrate binding => ECO:0000269|PubMed:18004778
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
4)
|
chain |
A |
residue |
276 |
type |
SITE |
sequence |
R
|
description |
Substrate binding => ECO:0000269|PubMed:18004778
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
5)
|
chain |
A |
residue |
270 |
type |
SITE |
sequence |
R
|
description |
Involved in NS3 ATPase and RTPase activities => ECO:0000250|UniProtKB:P14335
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
6)
|
chain |
A |
residue |
431 |
type |
SITE |
sequence |
R
|
description |
Cleavage; by autolysis => ECO:0000250|UniProtKB:P06935
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
7)
|
chain |
A |
residue |
204 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine; by host => ECO:0000250|UniProtKB:Q32ZE1
|
source |
Swiss-Prot : SWS_FT_FI5
|
|