|
|
1)
|
chain |
B |
residue |
85 |
type |
|
sequence |
Y
|
description |
IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT
|
source |
: ACT
|
|
2)
|
chain |
A |
residue |
121 |
type |
|
sequence |
T
|
description |
IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT
|
source |
: ACT
|
|
3)
|
chain |
A |
residue |
202 |
type |
|
sequence |
N
|
description |
IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT
|
source |
: ACT
|
|
4)
|
chain |
A |
residue |
230 |
type |
|
sequence |
D
|
description |
IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT
|
source |
: ACT
|
|
5)
|
chain |
A |
residue |
233 |
type |
|
sequence |
Y
|
description |
IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT
|
source |
: ACT
|
|
6)
|
chain |
A |
residue |
270 |
type |
|
sequence |
S
|
description |
IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT
|
source |
: ACT
|
|
7)
|
chain |
A |
residue |
273 |
type |
|
sequence |
K
|
description |
IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT
|
source |
: ACT
|
|
8)
|
chain |
A |
residue |
281 |
type |
|
sequence |
R
|
description |
IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT
|
source |
: ACT
|
|
9)
|
chain |
A |
residue |
407 |
type |
|
sequence |
R
|
description |
IN THE ACTIVE SITE OF ONE SUBUNIT, TYR 85 IS CONTRIBUTED BY THE OPPOSITE SUBUNIT
|
source |
: ACT
|
|
10)
|
chain |
A |
residue |
119 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE PLP A 500
|
source |
: AC1
|
|
11)
|
chain |
A |
residue |
120 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE PLP A 500
|
source |
: AC1
|
|
12)
|
chain |
A |
residue |
121 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE PLP A 500
|
source |
: AC1
|
|
13)
|
chain |
A |
residue |
145 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE PLP A 500
|
source |
: AC1
|
|
14)
|
chain |
A |
residue |
202 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE PLP A 500
|
source |
: AC1
|
|
15)
|
chain |
A |
residue |
230 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE PLP A 500
|
source |
: AC1
|
|
16)
|
chain |
A |
residue |
232 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE PLP A 500
|
source |
: AC1
|
|
17)
|
chain |
A |
residue |
233 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE PLP A 500
|
source |
: AC1
|
|
18)
|
chain |
A |
residue |
270 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE PLP A 500
|
source |
: AC1
|
|
19)
|
chain |
A |
residue |
272 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE PLP A 500
|
source |
: AC1
|
|
20)
|
chain |
A |
residue |
273 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE PLP A 500
|
source |
: AC1
|
|
21)
|
chain |
A |
residue |
281 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE PLP A 500
|
source |
: AC1
|
|
22)
|
chain |
B |
residue |
119 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE PLP B 500
|
source |
: AC2
|
|
23)
|
chain |
B |
residue |
120 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE PLP B 500
|
source |
: AC2
|
|
24)
|
chain |
B |
residue |
121 |
type |
|
sequence |
T
|
description |
BINDING SITE FOR RESIDUE PLP B 500
|
source |
: AC2
|
|
25)
|
chain |
B |
residue |
145 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE PLP B 500
|
source |
: AC2
|
|
26)
|
chain |
B |
residue |
202 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE PLP B 500
|
source |
: AC2
|
|
27)
|
chain |
B |
residue |
232 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE PLP B 500
|
source |
: AC2
|
|
28)
|
chain |
B |
residue |
233 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE PLP B 500
|
source |
: AC2
|
|
29)
|
chain |
B |
residue |
270 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE PLP B 500
|
source |
: AC2
|
|
30)
|
chain |
B |
residue |
272 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE PLP B 500
|
source |
: AC2
|
|
31)
|
chain |
B |
residue |
273 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE PLP B 500
|
source |
: AC2
|
|
32)
|
chain |
B |
residue |
281 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE PLP B 500
|
source |
: AC2
|
|
33)
|
chain |
A |
residue |
145 |
type |
catalytic |
sequence |
Y
|
description |
418
|
source |
MCSA : MCSA1
|
|
34)
|
chain |
A |
residue |
230 |
type |
catalytic |
sequence |
D
|
description |
418
|
source |
MCSA : MCSA1
|
|
35)
|
chain |
A |
residue |
232 |
type |
catalytic |
sequence |
I
|
description |
418
|
source |
MCSA : MCSA1
|
|
36)
|
chain |
A |
residue |
273 |
type |
catalytic |
sequence |
K
|
description |
418
|
source |
MCSA : MCSA1
|
|
37)
|
chain |
B |
residue |
145 |
type |
catalytic |
sequence |
Y
|
description |
418
|
source |
MCSA : MCSA2
|
|
38)
|
chain |
B |
residue |
230 |
type |
catalytic |
sequence |
D
|
description |
418
|
source |
MCSA : MCSA2
|
|
39)
|
chain |
B |
residue |
232 |
type |
catalytic |
sequence |
I
|
description |
418
|
source |
MCSA : MCSA2
|
|
40)
|
chain |
B |
residue |
273 |
type |
catalytic |
sequence |
K
|
description |
418
|
source |
MCSA : MCSA2
|
|
41)
|
chain |
A |
residue |
270-283 |
type |
prosite |
sequence |
SLSKDLGLPGFRVG
|
description |
AA_TRANSFER_CLASS_1 Aminotransferases class-I pyridoxal-phosphate attachment site. SLSKdlGLpGFRVG
|
source |
prosite : PS00105
|
|
42)
|
chain |
A |
residue |
84 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1M4N
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
43)
|
chain |
B |
residue |
84 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1M4N
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
44)
|
chain |
A |
residue |
145 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:1M4N
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
45)
|
chain |
A |
residue |
151 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:1M4N
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
46)
|
chain |
B |
residue |
145 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:1M4N
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
47)
|
chain |
B |
residue |
151 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000305|PubMed:12686108, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:1M4N
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
48)
|
chain |
A |
residue |
273 |
type |
MOD_RES |
sequence |
K
|
description |
N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10610793, ECO:0000269|PubMed:9398277, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:3PIU
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
49)
|
chain |
B |
residue |
273 |
type |
MOD_RES |
sequence |
K
|
description |
N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:10610793, ECO:0000269|PubMed:9398277, ECO:0007744|PDB:1B8G, ECO:0007744|PDB:3PIU
|
source |
Swiss-Prot : SWS_FT_FI3
|
|