|
|
1)
|
chain |
A |
residue |
51 |
type |
|
sequence |
T
|
description |
binding site for residue 9LQ A 401
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
52 |
type |
|
sequence |
G
|
description |
binding site for residue 9LQ A 401
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
57 |
type |
|
sequence |
V
|
description |
binding site for residue 9LQ A 401
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
70 |
type |
|
sequence |
A
|
description |
binding site for residue 9LQ A 401
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
72 |
type |
|
sequence |
K
|
description |
binding site for residue 9LQ A 401
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
121 |
type |
|
sequence |
E
|
description |
binding site for residue 9LQ A 401
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
122 |
type |
|
sequence |
Y
|
description |
binding site for residue 9LQ A 401
|
source |
: AC1
|
|
8)
|
chain |
A |
residue |
123 |
type |
|
sequence |
V
|
description |
binding site for residue 9LQ A 401
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
173 |
type |
|
sequence |
L
|
description |
binding site for residue 9LQ A 401
|
source |
: AC1
|
|
10)
|
chain |
A |
residue |
184 |
type |
|
sequence |
D
|
description |
binding site for residue 9LQ A 401
|
source |
: AC1
|
|
11)
|
chain |
A |
residue |
49-72 |
type |
prosite |
sequence |
LGTGSFGRVMLVKHKETGNHYAMK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGSFGRVMlVkhketgnh..........YAMK
|
source |
prosite : PS00107
|
|
12)
|
chain |
A |
residue |
162-174 |
type |
prosite |
sequence |
LIYRDLKPENLLI
|
description |
PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDLKpeNLLI
|
source |
prosite : PS00108
|
|
13)
|
chain |
A |
residue |
166 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
14)
|
chain |
A |
residue |
49 |
type |
BINDING |
sequence |
L
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
15)
|
chain |
A |
residue |
72 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
16)
|
chain |
A |
residue |
121 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
17)
|
chain |
A |
residue |
168 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
18)
|
chain |
A |
residue |
10 |
type |
MOD_RES |
sequence |
X
|
description |
Phosphoserine; by autocatalysis => ECO:0000250|UniProtKB:P05132
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
19)
|
chain |
A |
residue |
48 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0000250|UniProtKB:P17612
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
20)
|
chain |
A |
residue |
195 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0000250|UniProtKB:P17612
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
21)
|
chain |
A |
residue |
139 |
type |
MOD_RES |
sequence |
X
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P05132
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
22)
|
chain |
A |
residue |
197 |
type |
MOD_RES |
sequence |
X
|
description |
Phosphothreonine; by PDPK1 => ECO:0000250|UniProtKB:P00517
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
23)
|
chain |
A |
residue |
330 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:P05132
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
24)
|
chain |
A |
residue |
338 |
type |
MOD_RES |
sequence |
X
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P00517
|
source |
Swiss-Prot : SWS_FT_FI9
|
|