|
|
1)
|
chain |
A |
residue |
100 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE SO4 A 322
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
101 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE SO4 A 322
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
102 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE SO4 A 322
|
source |
: AC1
|
|
4)
|
chain |
B |
residue |
99 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE SO4 B 322
|
source |
: AC2
|
|
5)
|
chain |
B |
residue |
100 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE SO4 B 322
|
source |
: AC2
|
|
6)
|
chain |
B |
residue |
101 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE SO4 B 322
|
source |
: AC2
|
|
7)
|
chain |
B |
residue |
102 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE SO4 B 322
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
241 |
type |
catalytic |
sequence |
G
|
description |
571
|
source |
MCSA : MCSA1
|
|
9)
|
chain |
A |
residue |
270 |
type |
catalytic |
sequence |
P
|
description |
571
|
source |
MCSA : MCSA1
|
|
10)
|
chain |
A |
residue |
288 |
type |
catalytic |
sequence |
I
|
description |
571
|
source |
MCSA : MCSA1
|
|
11)
|
chain |
B |
residue |
241 |
type |
catalytic |
sequence |
G
|
description |
571
|
source |
MCSA : MCSA2
|
|
12)
|
chain |
B |
residue |
270 |
type |
catalytic |
sequence |
P
|
description |
571
|
source |
MCSA : MCSA2
|
|
13)
|
chain |
B |
residue |
288 |
type |
catalytic |
sequence |
I
|
description |
571
|
source |
MCSA : MCSA2
|
|
14)
|
chain |
A |
residue |
241 |
type |
ACT_SITE |
sequence |
G
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
15)
|
chain |
A |
residue |
270 |
type |
ACT_SITE |
sequence |
P
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
16)
|
chain |
B |
residue |
241 |
type |
ACT_SITE |
sequence |
G
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
17)
|
chain |
B |
residue |
270 |
type |
ACT_SITE |
sequence |
P
|
description |
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
18)
|
chain |
A |
residue |
288 |
type |
ACT_SITE |
sequence |
I
|
description |
Proton donor
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
19)
|
chain |
B |
residue |
288 |
type |
ACT_SITE |
sequence |
I
|
description |
Proton donor
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
20)
|
chain |
A |
residue |
158 |
type |
BINDING |
sequence |
I
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
21)
|
chain |
B |
residue |
288 |
type |
BINDING |
sequence |
I
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
22)
|
chain |
A |
residue |
178 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
23)
|
chain |
A |
residue |
239 |
type |
BINDING |
sequence |
A
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
24)
|
chain |
A |
residue |
265 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
25)
|
chain |
A |
residue |
288 |
type |
BINDING |
sequence |
I
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
26)
|
chain |
B |
residue |
158 |
type |
BINDING |
sequence |
I
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
27)
|
chain |
B |
residue |
178 |
type |
BINDING |
sequence |
T
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
28)
|
chain |
B |
residue |
239 |
type |
BINDING |
sequence |
A
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
29)
|
chain |
B |
residue |
265 |
type |
BINDING |
sequence |
V
|
description |
BINDING => ECO:0000250
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
30)
|
chain |
A |
residue |
150-177 |
type |
prosite |
sequence |
LGIYGFGSIGQALAKRAQGFDMDIDYFD
|
description |
D_2_HYDROXYACID_DH_1 D-isomer specific 2-hydroxyacid dehydrogenases NAD-binding signature. LGIYGfGSIGqalakraqgfdmd.IDyFD
|
source |
prosite : PS00065
|
|
31)
|
chain |
A |
residue |
200-222 |
type |
prosite |
sequence |
LLSVSQFFSLNAPSTPETRYFFN
|
description |
D_2_HYDROXYACID_DH_2 D-isomer specific 2-hydroxyacid dehydrogenases signature 2. LLsvSQFFsLNaPstpeTryFfN
|
source |
prosite : PS00670
|
|
32)
|
chain |
A |
residue |
229-245 |
type |
prosite |
sequence |
LPQGAIVVNTARGDLVD
|
description |
D_2_HYDROXYACID_DH_3 D-isomer specific 2-hydroxyacid dehydrogenases signature 3. LPqGaIVVNtARGdLVD
|
source |
prosite : PS00671
|
|