|
|
1)
|
chain |
C |
residue |
89 |
type |
|
sequence |
G
|
description |
binding site for residue ATP C 401
|
source |
: AC3
|
|
2)
|
chain |
C |
residue |
91 |
type |
|
sequence |
G
|
description |
binding site for residue ATP C 401
|
source |
: AC3
|
|
3)
|
chain |
C |
residue |
92 |
type |
|
sequence |
S
|
description |
binding site for residue ATP C 401
|
source |
: AC3
|
|
4)
|
chain |
C |
residue |
94 |
type |
|
sequence |
S
|
description |
binding site for residue ATP C 401
|
source |
: AC3
|
|
5)
|
chain |
C |
residue |
96 |
type |
|
sequence |
V
|
description |
binding site for residue ATP C 401
|
source |
: AC3
|
|
6)
|
chain |
C |
residue |
109 |
type |
|
sequence |
A
|
description |
binding site for residue ATP C 401
|
source |
: AC3
|
|
7)
|
chain |
C |
residue |
111 |
type |
|
sequence |
K
|
description |
binding site for residue ATP C 401
|
source |
: AC3
|
|
8)
|
chain |
C |
residue |
160 |
type |
|
sequence |
S
|
description |
binding site for residue ATP C 401
|
source |
: AC3
|
|
9)
|
chain |
C |
residue |
162 |
type |
|
sequence |
A
|
description |
binding site for residue ATP C 401
|
source |
: AC3
|
|
10)
|
chain |
C |
residue |
166 |
type |
|
sequence |
E
|
description |
binding site for residue ATP C 401
|
source |
: AC3
|
|
11)
|
chain |
C |
residue |
209 |
type |
|
sequence |
E
|
description |
binding site for residue ATP C 401
|
source |
: AC3
|
|
12)
|
chain |
C |
residue |
212 |
type |
|
sequence |
L
|
description |
binding site for residue ATP C 401
|
source |
: AC3
|
|
13)
|
chain |
C |
residue |
144 |
type |
|
sequence |
K
|
description |
binding site for residue CL C 402
|
source |
: AC4
|
|
14)
|
chain |
C |
residue |
131 |
type |
|
sequence |
R
|
description |
binding site for Di-peptide PHE E 11 and SEP E 12
|
source |
: AC6
|
|
15)
|
chain |
C |
residue |
148 |
type |
|
sequence |
T
|
description |
binding site for Di-peptide PHE E 11 and SEP E 12
|
source |
: AC6
|
|
16)
|
chain |
C |
residue |
149 |
type |
|
sequence |
F
|
description |
binding site for Di-peptide PHE E 11 and SEP E 12
|
source |
: AC6
|
|
17)
|
chain |
C |
residue |
150 |
type |
|
sequence |
Q
|
description |
binding site for Di-peptide PHE E 11 and SEP E 12
|
source |
: AC6
|
|
18)
|
chain |
C |
residue |
145 |
type |
|
sequence |
L
|
description |
binding site for Di-peptide SEP E 12 and TYR E 13
|
source |
: AC7
|
|
19)
|
chain |
C |
residue |
147 |
type |
|
sequence |
F
|
description |
binding site for Di-peptide SEP E 12 and TYR E 13
|
source |
: AC7
|
|
20)
|
chain |
C |
residue |
148 |
type |
|
sequence |
T
|
description |
binding site for Di-peptide SEP E 12 and TYR E 13
|
source |
: AC7
|
|
21)
|
chain |
C |
residue |
150 |
type |
|
sequence |
Q
|
description |
binding site for Di-peptide SEP E 12 and TYR E 13
|
source |
: AC7
|
|
22)
|
chain |
C |
residue |
205 |
type |
ACT_SITE |
sequence |
D
|
description |
Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
23)
|
chain |
C |
residue |
92 |
type |
BINDING |
sequence |
S
|
description |
BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
24)
|
chain |
C |
residue |
111 |
type |
BINDING |
sequence |
K
|
description |
BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
25)
|
chain |
C |
residue |
160 |
type |
BINDING |
sequence |
S
|
description |
BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
26)
|
chain |
C |
residue |
166 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
27)
|
chain |
C |
residue |
223 |
type |
BINDING |
sequence |
D
|
description |
BINDING => ECO:0000269|PubMed:12169624, ECO:0000269|PubMed:15741170, ECO:0000269|PubMed:22999883
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
28)
|
chain |
C |
residue |
209 |
type |
BINDING |
sequence |
E
|
description |
BINDING => ECO:0000269|PubMed:22999883
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
29)
|
chain |
C |
residue |
241 |
type |
MOD_RES |
sequence |
X
|
description |
Phosphoserine; by autocatalysis => ECO:0000269|PubMed:10455013, ECO:0000269|PubMed:11481331, ECO:0000269|PubMed:15772071, ECO:0000269|PubMed:16780920, ECO:0000269|Ref.8
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
30)
|
chain |
C |
residue |
304 |
type |
MOD_RES |
sequence |
K
|
description |
N6-acetyllysine => ECO:0000250|UniProtKB:Q9Z2A0
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
31)
|
chain |
C |
residue |
354 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine; by MELK => ECO:0000269|PubMed:22544756
|
source |
Swiss-Prot : SWS_FT_FI6
|
|