|
|
1)
|
chain |
A |
residue |
378 |
type |
catalytic |
sequence |
T
|
description |
205
|
source |
MCSA : MCSA1
|
|
2)
|
chain |
A |
residue |
569 |
type |
catalytic |
sequence |
R
|
description |
205
|
source |
MCSA : MCSA1
|
|
3)
|
chain |
A |
residue |
570 |
type |
catalytic |
sequence |
I
|
description |
205
|
source |
MCSA : MCSA1
|
|
4)
|
chain |
A |
residue |
575 |
type |
catalytic |
sequence |
R
|
description |
205
|
source |
MCSA : MCSA1
|
|
5)
|
chain |
A |
residue |
677 |
type |
catalytic |
sequence |
G
|
description |
205
|
source |
MCSA : MCSA1
|
|
6)
|
chain |
A |
residue |
681 |
type |
catalytic |
sequence |
F
|
description |
205
|
source |
MCSA : MCSA1
|
|
7)
|
chain |
A |
residue |
672-684 |
type |
prosite |
sequence |
EASGTGNMKFMLN
|
description |
PHOSPHORYLASE Phosphorylase pyridoxal-phosphate attachment site. EASGtGnMKfmLN
|
source |
prosite : PS00102
|
|
8)
|
chain |
A |
residue |
43 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000250|UniProtKB:P11217
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
9)
|
chain |
A |
residue |
310 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000250|UniProtKB:P11217
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
10)
|
chain |
A |
residue |
514 |
type |
MOD_RES |
sequence |
D
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P09812
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
11)
|
chain |
A |
residue |
747 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P09812
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
12)
|
chain |
A |
residue |
748 |
type |
MOD_RES |
sequence |
G
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P09812
|
source |
Swiss-Prot : SWS_FT_FI10
|
|
13)
|
chain |
A |
residue |
681 |
type |
MOD_RES |
sequence |
F
|
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
|
|
14)
|
chain |
A |
residue |
76 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000269|PubMed:3616621
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
15)
|
chain |
A |
residue |
109 |
type |
SITE |
sequence |
D
|
description |
Involved in the association of subunits => ECO:0000303|PubMed:728424
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
16)
|
chain |
A |
residue |
143 |
type |
SITE |
sequence |
F
|
description |
Involved in the association of subunits => ECO:0000303|PubMed:728424
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
17)
|
chain |
A |
residue |
156 |
type |
SITE |
sequence |
G
|
description |
Can be labeled by an AMP analog; may be involved in allosteric regulation => ECO:0000303|PubMed:728424
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
18)
|
chain |
A |
residue |
15 |
type |
MOD_RES |
sequence |
V
|
description |
Phosphoserine; by PHK; in form phosphorylase A => ECO:0000250|UniProtKB:P11217
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
19)
|
chain |
A |
residue |
204 |
type |
MOD_RES |
sequence |
G
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:P09812
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
20)
|
chain |
A |
residue |
227 |
type |
MOD_RES |
sequence |
D
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:P09812
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
21)
|
chain |
A |
residue |
430 |
type |
MOD_RES |
sequence |
L
|
description |
Phosphoserine => ECO:0000250|UniProtKB:Q9WUB3
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
22)
|
chain |
A |
residue |
473 |
type |
MOD_RES |
sequence |
E
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:Q9WUB3
|
source |
Swiss-Prot : SWS_FT_FI9
|
|