|
|
1)
|
chain |
A |
residue |
162 |
type |
|
sequence |
D
|
description |
binding site for residue MN A 301
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
30 |
type |
|
sequence |
I
|
description |
binding site for residue 3FE A 302
|
source |
: AC2
|
|
3)
|
chain |
A |
residue |
31 |
type |
|
sequence |
G
|
description |
binding site for residue 3FE A 302
|
source |
: AC2
|
|
4)
|
chain |
A |
residue |
32 |
type |
|
sequence |
K
|
description |
binding site for residue 3FE A 302
|
source |
: AC2
|
|
5)
|
chain |
A |
residue |
51 |
type |
|
sequence |
A
|
description |
binding site for residue 3FE A 302
|
source |
: AC2
|
|
6)
|
chain |
A |
residue |
53 |
type |
|
sequence |
K
|
description |
binding site for residue 3FE A 302
|
source |
: AC2
|
|
7)
|
chain |
A |
residue |
70 |
type |
|
sequence |
E
|
description |
binding site for residue 3FE A 302
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
100 |
type |
|
sequence |
E
|
description |
binding site for residue 3FE A 302
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
101 |
type |
|
sequence |
Y
|
description |
binding site for residue 3FE A 302
|
source |
: AC2
|
|
10)
|
chain |
A |
residue |
102 |
type |
|
sequence |
L
|
description |
binding site for residue 3FE A 302
|
source |
: AC2
|
|
11)
|
chain |
A |
residue |
151 |
type |
|
sequence |
L
|
description |
binding site for residue 3FE A 302
|
source |
: AC2
|
|
12)
|
chain |
A |
residue |
161 |
type |
|
sequence |
A
|
description |
binding site for residue 3FE A 302
|
source |
: AC2
|
|
13)
|
chain |
A |
residue |
162 |
type |
|
sequence |
D
|
description |
binding site for residue 3FE A 302
|
source |
: AC2
|
|
14)
|
chain |
A |
residue |
178 |
type |
MOD_RES |
sequence |
X
|
description |
Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:17046825, ECO:0000269|PubMed:19604147, ECO:0000269|PubMed:20124694, ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
15)
|
chain |
A |
residue |
30-53 |
type |
prosite |
sequence |
IGKGSFGEVFKGIDNRTQKVVAIK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGEVFkGidnrtqkv..........VAIK
|
source |
prosite : PS00107
|
|
16)
|
chain |
A |
residue |
144 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
17)
|
chain |
A |
residue |
30 |
type |
BINDING |
sequence |
I
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
18)
|
chain |
A |
residue |
53 |
type |
BINDING |
sequence |
K
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
19)
|
chain |
A |
residue |
100 |
type |
BINDING |
sequence |
E
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
20)
|
chain |
A |
residue |
149 |
type |
BINDING |
sequence |
N
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
21)
|
chain |
A |
residue |
162 |
type |
BINDING |
sequence |
D
|
description |
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
22)
|
chain |
A |
residue |
18 |
type |
MOD_RES |
sequence |
A
|
description |
Phosphothreonine; by PKA => ECO:0000269|PubMed:10644707
|
source |
Swiss-Prot : SWS_FT_FI3
|
|