|
|
1)
|
chain |
A |
residue |
35 |
type |
|
sequence |
E
|
description |
binding site for residue DMS A 401
|
source |
: AC1
|
|
2)
|
chain |
A |
residue |
36 |
type |
|
sequence |
M
|
description |
binding site for residue DMS A 401
|
source |
: AC1
|
|
3)
|
chain |
A |
residue |
73 |
type |
|
sequence |
Y
|
description |
binding site for residue DMS A 401
|
source |
: AC1
|
|
4)
|
chain |
A |
residue |
88 |
type |
|
sequence |
Y
|
description |
binding site for residue DMS A 401
|
source |
: AC1
|
|
5)
|
chain |
A |
residue |
142 |
type |
|
sequence |
E
|
description |
binding site for residue DMS A 401
|
source |
: AC1
|
|
6)
|
chain |
A |
residue |
326 |
type |
|
sequence |
R
|
description |
binding site for residue DMS A 401
|
source |
: AC1
|
|
7)
|
chain |
A |
residue |
114 |
type |
|
sequence |
R
|
description |
binding site for residue CL A 402
|
source |
: AC2
|
|
8)
|
chain |
A |
residue |
272 |
type |
|
sequence |
E
|
description |
binding site for residue CL A 402
|
source |
: AC2
|
|
9)
|
chain |
A |
residue |
2 |
type |
|
sequence |
K
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
10)
|
chain |
A |
residue |
15 |
type |
|
sequence |
E
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
11)
|
chain |
A |
residue |
17 |
type |
|
sequence |
I
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
12)
|
chain |
A |
residue |
18 |
type |
|
sequence |
G
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
13)
|
chain |
A |
residue |
25 |
type |
|
sequence |
V
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
14)
|
chain |
A |
residue |
38 |
type |
|
sequence |
A
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
15)
|
chain |
A |
residue |
40 |
type |
|
sequence |
K
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
16)
|
chain |
A |
residue |
57 |
type |
|
sequence |
E
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
17)
|
chain |
A |
residue |
86 |
type |
|
sequence |
L
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
18)
|
chain |
A |
residue |
87 |
type |
|
sequence |
E
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
19)
|
chain |
A |
residue |
88 |
type |
|
sequence |
Y
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
20)
|
chain |
A |
residue |
89 |
type |
|
sequence |
C
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
21)
|
chain |
A |
residue |
92 |
type |
|
sequence |
G
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
22)
|
chain |
A |
residue |
93 |
type |
|
sequence |
E
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
23)
|
chain |
A |
residue |
139 |
type |
|
sequence |
L
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
24)
|
chain |
A |
residue |
149 |
type |
|
sequence |
I
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
25)
|
chain |
A |
residue |
150 |
type |
|
sequence |
D
|
description |
binding site for residue XIN A 403
|
source |
: AC3
|
|
26)
|
chain |
A |
residue |
132 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
27)
|
chain |
A |
residue |
17 |
type |
BINDING |
sequence |
I
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
28)
|
chain |
A |
residue |
40 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
29)
|
chain |
A |
residue |
56 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:16216881
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
30)
|
chain |
A |
residue |
17-40 |
type |
prosite |
sequence |
IGTGGFAKVKLACHILTGEMVAIK
|
description |
PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGTGGFAKVKlAchiltgem..........VAIK
|
source |
prosite : PS00107
|
|
31)
|
chain |
A |
residue |
128-140 |
type |
prosite |
sequence |
YAHRDLKPENLLF
|
description |
PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. YaHrDLKpeNLLF
|
source |
prosite : PS00108
|
|
32)
|
chain |
A |
residue |
171 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine; by autocatalysis => ECO:0000269|PubMed:16216881
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
33)
|
chain |
A |
residue |
253 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine; by autocatalysis => ECO:0000269|PubMed:16216881
|
source |
Swiss-Prot : SWS_FT_FI6
|
|