|
|
1)
|
chain |
X |
residue |
249 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE GOL X 401
|
source |
: AC1
|
|
2)
|
chain |
X |
residue |
250 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE GOL X 401
|
source |
: AC1
|
|
3)
|
chain |
X |
residue |
278 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE GOL X 401
|
source |
: AC1
|
|
4)
|
chain |
X |
residue |
282 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE GOL X 401
|
source |
: AC1
|
|
5)
|
chain |
X |
residue |
7 |
type |
BINDING |
sequence |
N
|
description |
BINDING => ECO:0000250|UniProtKB:P0A1E3
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
6)
|
chain |
X |
residue |
268 |
type |
BINDING |
sequence |
L
|
description |
in other chain => ECO:0000250|UniProtKB:P0A1E3
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
7)
|
chain |
X |
residue |
35 |
type |
BINDING |
sequence |
R
|
description |
in other chain => ECO:0000250|UniProtKB:P0A1E3
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
8)
|
chain |
X |
residue |
272 |
type |
BINDING |
sequence |
S
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
9)
|
chain |
X |
residue |
177 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
10)
|
chain |
X |
residue |
72 |
type |
BINDING |
sequence |
N
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
11)
|
chain |
X |
residue |
42 |
type |
MOD_RES |
sequence |
X
|
description |
N6-(pyridoxal phosphate)lysine => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
12)
|
chain |
X |
residue |
31-49 |
type |
prosite |
sequence |
KIEGRNPSYSVXCRIGANM
|
description |
CYS_SYNTHASE Cysteine synthase/cystathionine beta-synthase P-phosphate attachment site. KiEgrn.PSySVKcRiGanM
|
source |
prosite : PS00901
|
|