|
|
1)
|
chain |
A |
residue |
79 |
type |
|
sequence |
C
|
description |
BINDING SITE FOR RESIDUE IOD A 301
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
78 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE IOD A 303
|
source |
: AC2
|
|
3)
|
chain |
A |
residue |
171 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE IOD A 304
|
source |
: AC3
|
|
4)
|
chain |
A |
residue |
175 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE IOD A 304
|
source |
: AC3
|
|
5)
|
chain |
A |
residue |
201 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE IOD A 305
|
source |
: AC4
|
|
6)
|
chain |
A |
residue |
73 |
type |
ACT_SITE |
sequence |
C
|
description |
Proton donor => ECO:0000255|HAMAP-Rule:MF_00197
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
7)
|
chain |
A |
residue |
217 |
type |
ACT_SITE |
sequence |
C
|
description |
Proton acceptor => ECO:0000255|HAMAP-Rule:MF_00197
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
8)
|
chain |
A |
residue |
64 |
type |
BINDING |
sequence |
N
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00197
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
9)
|
chain |
A |
residue |
74 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00197
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
10)
|
chain |
A |
residue |
157 |
type |
BINDING |
sequence |
N
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00197
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
11)
|
chain |
A |
residue |
190 |
type |
BINDING |
sequence |
N
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00197
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
12)
|
chain |
A |
residue |
208 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00197
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
13)
|
chain |
A |
residue |
218 |
type |
BINDING |
sequence |
G
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00197
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
14)
|
chain |
A |
residue |
11 |
type |
BINDING |
sequence |
N
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00197
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
15)
|
chain |
A |
residue |
44 |
type |
BINDING |
sequence |
Q
|
description |
BINDING => ECO:0000255|HAMAP-Rule:MF_00197
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
16)
|
chain |
A |
residue |
159 |
type |
SITE |
sequence |
H
|
description |
Could be important to modulate the pK values of the two catalytic cysteine residues => ECO:0000255|HAMAP-Rule:MF_00197
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
17)
|
chain |
A |
residue |
208 |
type |
SITE |
sequence |
E
|
description |
Could be important to modulate the pK values of the two catalytic cysteine residues => ECO:0000255|HAMAP-Rule:MF_00197
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
18)
|
chain |
A |
residue |
268 |
type |
SITE |
sequence |
A
|
description |
Important for dimerization => ECO:0000269|PubMed:23426375
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
19)
|
chain |
A |
residue |
64-78 |
type |
prosite |
sequence |
NADGSEVAQCGNGAR
|
description |
DAP_EPIMERASE Diaminopimelate epimerase signature. NaDGSevaqCGNGaR
|
source |
prosite : PS01326
|
|