|
|
1)
|
chain |
A |
residue |
1002 |
type |
|
sequence |
L
|
description |
BINDING SITE FOR RESIDUE 351 A2001
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
1028 |
type |
|
sequence |
A
|
description |
BINDING SITE FOR RESIDUE 351 A2001
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
1030 |
type |
|
sequence |
K
|
description |
BINDING SITE FOR RESIDUE 351 A2001
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
1047 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE 351 A2001
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
1051 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE 351 A2001
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
1059 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE 351 A2001
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
1060 |
type |
|
sequence |
V
|
description |
BINDING SITE FOR RESIDUE 351 A2001
|
source |
: AC1
|
|
8)
|
chain |
A |
residue |
1077 |
type |
|
sequence |
E
|
description |
BINDING SITE FOR RESIDUE 351 A2001
|
source |
: AC1
|
|
9)
|
chain |
A |
residue |
1079 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE 351 A2001
|
source |
: AC1
|
|
10)
|
chain |
A |
residue |
1128 |
type |
|
sequence |
F
|
description |
BINDING SITE FOR RESIDUE 351 A2001
|
source |
: AC1
|
|
11)
|
chain |
A |
residue |
1139 |
type |
|
sequence |
M
|
description |
BINDING SITE FOR RESIDUE 351 A2001
|
source |
: AC1
|
|
12)
|
chain |
A |
residue |
1148 |
type |
|
sequence |
I
|
description |
BINDING SITE FOR RESIDUE 351 A2001
|
source |
: AC1
|
|
13)
|
chain |
A |
residue |
1149 |
type |
|
sequence |
G
|
description |
BINDING SITE FOR RESIDUE 351 A2001
|
source |
: AC1
|
|
14)
|
chain |
A |
residue |
1150 |
type |
|
sequence |
D
|
description |
BINDING SITE FOR RESIDUE 351 A2001
|
source |
: AC1
|
|
15)
|
chain |
A |
residue |
1132 |
type |
catalytic |
sequence |
D
|
description |
246
|
source |
MCSA : MCSA1
|
|
16)
|
chain |
A |
residue |
1136 |
type |
catalytic |
sequence |
R
|
description |
246
|
source |
MCSA : MCSA1
|
|
17)
|
chain |
A |
residue |
1137 |
type |
catalytic |
sequence |
N
|
description |
246
|
source |
MCSA : MCSA1
|
|
18)
|
chain |
A |
residue |
1150 |
type |
catalytic |
sequence |
D
|
description |
246
|
source |
MCSA : MCSA1
|
|
19)
|
chain |
A |
residue |
1158 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
20)
|
chain |
A |
residue |
1162 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
21)
|
chain |
A |
residue |
1163 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:14690593, ECO:0000269|PubMed:16246733, ECO:0000269|PubMed:16271887, ECO:0000269|PubMed:18278056, ECO:0000269|PubMed:18767165, ECO:0000269|PubMed:3166375, ECO:0000269|PubMed:9312016
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
22)
|
chain |
A |
residue |
1002-1030 |
type |
prosite |
sequence |
LGQGSFGMVYEGNARDIIKGEAETRVAVK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGMVYeGnardiikgeaetr.....VAVK
|
source |
prosite : PS00107
|
|
23)
|
chain |
A |
residue |
1128-1140 |
type |
prosite |
sequence |
FVHRDLAARNCMV
|
description |
PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNCMV
|
source |
prosite : PS00109
|
|
24)
|
chain |
A |
residue |
1156-1164 |
type |
prosite |
sequence |
DIYETDYYR
|
description |
RECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. DIYetdYYR
|
source |
prosite : PS00239
|
|
25)
|
chain |
A |
residue |
1132 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton donor/acceptor => ECO:0000269|PubMed:9312016
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
26)
|
chain |
A |
residue |
1006 |
type |
BINDING |
sequence |
S
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
27)
|
chain |
A |
residue |
1030 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
28)
|
chain |
A |
residue |
1077 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
29)
|
chain |
A |
residue |
1136 |
type |
BINDING |
sequence |
R
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
30)
|
chain |
A |
residue |
1150 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:18278056
|
source |
Swiss-Prot : SWS_FT_FI2
|
|