|
|
1)
|
chain |
A |
residue |
88 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE F59 A 998
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
133 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE F59 A 998
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
135 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE F59 A 998
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
136 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE F59 A 998
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
282 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE F59 A 998
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
292 |
type |
|
sequence |
R
|
description |
BINDING SITE FOR RESIDUE F59 A 998
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
341 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE F59 A 998
|
source |
: AC1
|
|
8)
|
chain |
A |
residue |
377 |
type |
|
sequence |
H
|
description |
BINDING SITE FOR RESIDUE F59 A 998
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
385 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE F59 A 998
|
source |
: AC1
|
|
10)
|
chain |
A |
residue |
484 |
type |
|
sequence |
N
|
description |
BINDING SITE FOR RESIDUE F59 A 998
|
source |
: AC1
|
|
11)
|
chain |
A |
residue |
573 |
type |
|
sequence |
Y
|
description |
BINDING SITE FOR RESIDUE F59 A 998
|
source |
: AC1
|
|
12)
|
chain |
A |
residue |
672 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE F59 A 998
|
source |
: AC1
|
|
13)
|
chain |
A |
residue |
673 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE F59 A 998
|
source |
: AC1
|
|
14)
|
chain |
A |
residue |
674 |
type |
|
sequence |
S
|
description |
BINDING SITE FOR RESIDUE F59 A 998
|
source |
: AC1
|
|
15)
|
chain |
A |
residue |
675 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE F59 A 998
|
source |
: AC1
|
|
16)
|
chain |
A |
residue |
377 |
type |
catalytic |
sequence |
H
|
description |
205
|
source |
MCSA : MCSA1
|
|
17)
|
chain |
A |
residue |
568 |
type |
catalytic |
sequence |
K
|
description |
205
|
source |
MCSA : MCSA1
|
|
18)
|
chain |
A |
residue |
569 |
type |
catalytic |
sequence |
R
|
description |
205
|
source |
MCSA : MCSA1
|
|
19)
|
chain |
A |
residue |
574 |
type |
catalytic |
sequence |
K
|
description |
205
|
source |
MCSA : MCSA1
|
|
20)
|
chain |
A |
residue |
676 |
type |
catalytic |
sequence |
T
|
description |
205
|
source |
MCSA : MCSA1
|
|
21)
|
chain |
A |
residue |
680 |
type |
catalytic |
sequence |
X
|
description |
205
|
source |
MCSA : MCSA1
|
|
22)
|
chain |
A |
residue |
513 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P09812
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
23)
|
chain |
A |
residue |
746 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P09812
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
24)
|
chain |
A |
residue |
747 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P09812
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
25)
|
chain |
A |
residue |
680 |
type |
MOD_RES |
sequence |
X
|
description |
N6-(pyridoxal phosphate)lysine => ECO:0000269|PubMed:7500360, ECO:0000269|PubMed:8976550, ECO:0007744|PDB:2PRI, ECO:0007744|PDB:2SKC, ECO:0007744|PDB:2SKD, ECO:0007744|PDB:2SKE
|
source |
Swiss-Prot : SWS_FT_FI11
|
|
26)
|
chain |
A |
residue |
108 |
type |
SITE |
sequence |
C
|
description |
Involved in the association of subunits => ECO:0000303|PubMed:728424
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
27)
|
chain |
A |
residue |
142 |
type |
SITE |
sequence |
C
|
description |
Involved in the association of subunits => ECO:0000303|PubMed:728424
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
28)
|
chain |
A |
residue |
14 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
29)
|
chain |
A |
residue |
203 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:P09812
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
30)
|
chain |
A |
residue |
226 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:P09812
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
31)
|
chain |
A |
residue |
429 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
32)
|
chain |
A |
residue |
472 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
33)
|
chain |
A |
residue |
672-684 |
type |
prosite |
sequence |
EASGTGNMXFMLN
|
description |
PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN
|
source |
prosite : PS00102
|
|
34)
|
chain |
A |
residue |
42 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000250|UniProtKB:P11217
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
35)
|
chain |
A |
residue |
309 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000250|UniProtKB:P11217
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
36)
|
chain |
A |
residue |
75 |
type |
BINDING |
sequence |
Y
|
description |
BINDING => ECO:0000269|PubMed:3616621
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
37)
|
chain |
A |
residue |
155 |
type |
SITE |
sequence |
Y
|
description |
Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424
|
source |
Swiss-Prot : SWS_FT_FI4
|
|