|
|
1)
|
chain |
C |
residue |
495 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE CIT C 601
|
source |
: AC1
|
|
2)
|
chain |
C |
residue |
519 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE CIT C 601
|
source |
: AC1
|
|
3)
|
chain |
C |
residue |
544 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE CIT C 601
|
source |
: AC1
|
|
4)
|
chain |
C |
residue |
545 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE CIT C 601
|
source |
: AC1
|
|
5)
|
chain |
C |
residue |
546 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE CIT C 601
|
source |
: AC1
|
|
6)
|
chain |
C |
residue |
510 |
type |
catalytic |
sequence |
D
|
description |
530
|
source |
MCSA : MCSA2
|
|
7)
|
chain |
C |
residue |
513 |
type |
catalytic |
sequence |
H
|
description |
530
|
source |
MCSA : MCSA2
|
|
8)
|
chain |
C |
residue |
517 |
type |
catalytic |
sequence |
E
|
description |
530
|
source |
MCSA : MCSA2
|
|
9)
|
chain |
C |
residue |
545 |
type |
catalytic |
sequence |
R
|
description |
530
|
source |
MCSA : MCSA2
|
|
10)
|
chain |
C |
residue |
513 |
type |
ACT_SITE |
sequence |
H
|
description |
Proton donor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
11)
|
chain |
C |
residue |
517 |
type |
ACT_SITE |
sequence |
E
|
description |
Proton acceptor => ECO:0000305|PubMed:11741540, ECO:0000305|PubMed:20852642
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
12)
|
chain |
C |
residue |
545 |
type |
ACT_SITE |
sequence |
R
|
description |
ACT_SITE => ECO:0000305|PubMed:11741540
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
13)
|
chain |
C |
residue |
510 |
type |
SITE |
sequence |
D
|
description |
Stabilizes positive charge on His-513 => ECO:0000305|PubMed:20852642
|
source |
Swiss-Prot : SWS_FT_FI4
|
|