|
|
1)
|
chain |
A |
residue |
44 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE UGX A 1306
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
45 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE UGX A 1306
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
49 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE UGX A 1306
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
65 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE UGX A 1306
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
67 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE UGX A 1306
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
120 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE UGX A 1306
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
121 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE UGX A 1306
|
source |
: AC1
|
|
8)
|
chain |
A |
residue |
128 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE UGX A 1306
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
174 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE UGX A 1306
|
source |
: AC1
|
|
10)
|
chain |
A |
residue |
185 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE UGX A 1306
|
source |
: AC1
|
|
11)
|
chain |
A |
residue |
186 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE UGX A 1306
|
source |
: AC1
|
|
12)
|
chain |
A |
residue |
44-67 |
type |
prosite |
sequence |
LGSGGFGSVYSGIRVSDNLPVAIK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGGFGSVYsGirvsdnlp..........VAIK
|
source |
prosite : PS00107
|
|
13)
|
chain |
A |
residue |
163-175 |
type |
prosite |
sequence |
VLHRDIKDENILI
|
description |
PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VlHrDIKdeNILI
|
source |
prosite : PS00108
|
|
14)
|
chain |
A |
residue |
167 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
15)
|
chain |
A |
residue |
44 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
16)
|
chain |
A |
residue |
67 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
17)
|
chain |
A |
residue |
121 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
18)
|
chain |
A |
residue |
128 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000305|PubMed:15525646, ECO:0000305|PubMed:15657054, ECO:0000305|PubMed:15808862
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
19)
|
chain |
A |
residue |
98 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000269|PubMed:15657054
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
20)
|
chain |
A |
residue |
261 |
type |
MOD_RES |
sequence |
X
|
description |
Phosphoserine => ECO:0000269|PubMed:15657054
|
source |
Swiss-Prot : SWS_FT_FI6
|
|