|
|
1)
|
chain |
B |
residue |
6 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE KEG A 902
|
source |
: AC1
|
|
2)
|
chain |
B |
residue |
12 |
type |
|
sequence |
P
|
description |
BINDING SITE FOR RESIDUE KEG A 902
|
source |
: AC1
|
|
3)
|
chain |
B |
residue |
55 |
type |
|
sequence |
P
|
description |
BINDING SITE FOR RESIDUE KEG D 901
|
source |
: AC3
|
|
4)
|
chain |
B |
residue |
62 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE KEG D 901
|
source |
: AC3
|
|
5)
|
chain |
B |
residue |
64 |
type |
|
sequence |
Q
|
description |
BINDING SITE FOR RESIDUE KEG D 901
|
source |
: AC3
|
|
6)
|
chain |
B |
residue |
34 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
7)
|
chain |
B |
residue |
36 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
8)
|
chain |
B |
residue |
145 |
type |
BINDING |
sequence |
N
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
9)
|
chain |
B |
residue |
34 |
type |
ACT_SITE |
sequence |
D
|
description |
4-aspartylphosphate intermediate => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
10)
|
chain |
B |
residue |
36 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton donor => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
11)
|
chain |
B |
residue |
90 |
type |
SITE |
sequence |
T
|
description |
Transition state stabilizer => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
12)
|
chain |
B |
residue |
128 |
type |
SITE |
sequence |
K
|
description |
Transition state stabilizer => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI4
|
|