|
|
1)
|
chain |
A |
residue |
120 |
type |
|
sequence |
K
|
description |
binding site for residue NA A 301
|
source |
: AC1
|
|
2)
|
chain |
B |
residue |
202 |
type |
|
sequence |
D
|
description |
binding site for residue MG B 301
|
source |
: AC2
|
|
3)
|
chain |
B |
residue |
203 |
type |
|
sequence |
D
|
description |
binding site for residue MG B 301
|
source |
: AC2
|
|
4)
|
chain |
B |
residue |
204 |
type |
|
sequence |
A
|
description |
binding site for residue MG B 301
|
source |
: AC2
|
|
5)
|
chain |
B |
residue |
205 |
type |
|
sequence |
I
|
description |
binding site for residue MG B 301
|
source |
: AC2
|
|
6)
|
chain |
B |
residue |
206 |
type |
|
sequence |
A
|
description |
binding site for residue MG B 301
|
source |
: AC2
|
|
7)
|
chain |
B |
residue |
50 |
type |
|
sequence |
K
|
description |
binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
|
source |
: AC3
|
|
8)
|
chain |
B |
residue |
57 |
type |
|
sequence |
R
|
description |
binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
|
source |
: AC3
|
|
9)
|
chain |
B |
residue |
132 |
type |
|
sequence |
R
|
description |
binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
|
source |
: AC3
|
|
10)
|
chain |
B |
residue |
133 |
type |
|
sequence |
Y
|
description |
binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
|
source |
: AC3
|
|
11)
|
chain |
B |
residue |
174 |
type |
|
sequence |
G
|
description |
binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
|
source |
: AC3
|
|
12)
|
chain |
B |
residue |
177 |
type |
|
sequence |
L
|
description |
binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
|
source |
: AC3
|
|
13)
|
chain |
B |
residue |
178 |
type |
|
sequence |
N
|
description |
binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
|
source |
: AC3
|
|
14)
|
chain |
B |
residue |
225 |
type |
|
sequence |
L
|
description |
binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
|
source |
: AC3
|
|
15)
|
chain |
C |
residue |
5 |
type |
|
sequence |
S
|
description |
binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
|
source |
: AC3
|
|
16)
|
chain |
C |
residue |
8 |
type |
|
sequence |
P
|
description |
binding site for Ligand residues SEP C 6 through CYS C 7 bound to SER C 5
|
source |
: AC3
|
|
17)
|
chain |
A |
residue |
50 |
type |
|
sequence |
K
|
description |
binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
|
source |
: AC4
|
|
18)
|
chain |
A |
residue |
57 |
type |
|
sequence |
R
|
description |
binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
|
source |
: AC4
|
|
19)
|
chain |
A |
residue |
132 |
type |
|
sequence |
R
|
description |
binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
|
source |
: AC4
|
|
20)
|
chain |
A |
residue |
133 |
type |
|
sequence |
Y
|
description |
binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
|
source |
: AC4
|
|
21)
|
chain |
A |
residue |
174 |
type |
|
sequence |
G
|
description |
binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
|
source |
: AC4
|
|
22)
|
chain |
A |
residue |
177 |
type |
|
sequence |
L
|
description |
binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
|
source |
: AC4
|
|
23)
|
chain |
A |
residue |
178 |
type |
|
sequence |
N
|
description |
binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
|
source |
: AC4
|
|
24)
|
chain |
A |
residue |
225 |
type |
|
sequence |
L
|
description |
binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
|
source |
: AC4
|
|
25)
|
chain |
E |
residue |
5 |
type |
|
sequence |
S
|
description |
binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
|
source |
: AC4
|
|
26)
|
chain |
E |
residue |
8 |
type |
|
sequence |
P
|
description |
binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
|
source |
: AC4
|
|
27)
|
chain |
E |
residue |
9 |
type |
|
sequence |
A
|
description |
binding site for Ligand residues SEP E 6 through CYS E 7 bound to SER E 5
|
source |
: AC4
|
|
28)
|
chain |
D |
residue |
50 |
type |
|
sequence |
K
|
description |
binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
|
source |
: AC5
|
|
29)
|
chain |
D |
residue |
57 |
type |
|
sequence |
R
|
description |
binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
|
source |
: AC5
|
|
30)
|
chain |
D |
residue |
132 |
type |
|
sequence |
R
|
description |
binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
|
source |
: AC5
|
|
31)
|
chain |
D |
residue |
133 |
type |
|
sequence |
Y
|
description |
binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
|
source |
: AC5
|
|
32)
|
chain |
D |
residue |
174 |
type |
|
sequence |
G
|
description |
binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
|
source |
: AC5
|
|
33)
|
chain |
D |
residue |
177 |
type |
|
sequence |
L
|
description |
binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
|
source |
: AC5
|
|
34)
|
chain |
D |
residue |
178 |
type |
|
sequence |
N
|
description |
binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
|
source |
: AC5
|
|
35)
|
chain |
F |
residue |
5 |
type |
|
sequence |
S
|
description |
binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
|
source |
: AC5
|
|
36)
|
chain |
F |
residue |
8 |
type |
|
sequence |
P
|
description |
binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
|
source |
: AC5
|
|
37)
|
chain |
F |
residue |
9 |
type |
|
sequence |
A
|
description |
binding site for Ligand residues SEP F 6 through CYS F 7 bound to SER F 5
|
source |
: AC5
|
|
38)
|
chain |
G |
residue |
50 |
type |
|
sequence |
K
|
description |
binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
|
source |
: AC6
|
|
39)
|
chain |
G |
residue |
57 |
type |
|
sequence |
R
|
description |
binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
|
source |
: AC6
|
|
40)
|
chain |
G |
residue |
132 |
type |
|
sequence |
R
|
description |
binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
|
source |
: AC6
|
|
41)
|
chain |
G |
residue |
133 |
type |
|
sequence |
Y
|
description |
binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
|
source |
: AC6
|
|
42)
|
chain |
G |
residue |
174 |
type |
|
sequence |
G
|
description |
binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
|
source |
: AC6
|
|
43)
|
chain |
G |
residue |
177 |
type |
|
sequence |
L
|
description |
binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
|
source |
: AC6
|
|
44)
|
chain |
G |
residue |
178 |
type |
|
sequence |
N
|
description |
binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
|
source |
: AC6
|
|
45)
|
chain |
H |
residue |
5 |
type |
|
sequence |
S
|
description |
binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
|
source |
: AC6
|
|
46)
|
chain |
H |
residue |
8 |
type |
|
sequence |
P
|
description |
binding site for Ligand residues SEP H 6 through CYS H 7 bound to SER H 5
|
source |
: AC6
|
|
47)
|
chain |
A |
residue |
42-52 |
type |
prosite |
sequence |
RNLLSVAYKNV
|
description |
1433_1 14-3-3 proteins signature 1. RNLLSVAYKNV
|
source |
prosite : PS00796
|
|
48)
|
chain |
A |
residue |
216-235 |
type |
prosite |
sequence |
YKDSTLIMQLLRDNLTLWTS
|
description |
1433_2 14-3-3 proteins signature 2. YKDSTLIMQLLRDNLTLWTS
|
source |
prosite : PS00797
|
|
49)
|
chain |
A |
residue |
57 |
type |
SITE |
sequence |
R
|
description |
Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
50)
|
chain |
A |
residue |
132 |
type |
SITE |
sequence |
R
|
description |
Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
51)
|
chain |
B |
residue |
57 |
type |
SITE |
sequence |
R
|
description |
Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
52)
|
chain |
B |
residue |
132 |
type |
SITE |
sequence |
R
|
description |
Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
53)
|
chain |
D |
residue |
57 |
type |
SITE |
sequence |
R
|
description |
Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
54)
|
chain |
D |
residue |
132 |
type |
SITE |
sequence |
R
|
description |
Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
55)
|
chain |
G |
residue |
57 |
type |
SITE |
sequence |
R
|
description |
Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
56)
|
chain |
G |
residue |
132 |
type |
SITE |
sequence |
R
|
description |
Interaction with phosphoserine on interacting protein => ECO:0000269|PubMed:17085597
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
57)
|
chain |
A |
residue |
2 |
type |
MOD_RES |
sequence |
V
|
description |
N-acetylvaline; partial => ECO:0000269|PubMed:14534293, ECO:0000269|Ref.7, ECO:0000269|Ref.9, ECO:0007744|PubMed:19413330
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
58)
|
chain |
D |
residue |
71 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:23186163
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
59)
|
chain |
A |
residue |
133 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:P61983
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
60)
|
chain |
B |
residue |
133 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:P61983
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
61)
|
chain |
D |
residue |
133 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:P61983
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
62)
|
chain |
G |
residue |
133 |
type |
MOD_RES |
sequence |
Y
|
description |
Phosphotyrosine => ECO:0000250|UniProtKB:P61983
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
63)
|
chain |
A |
residue |
145 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0000269|Ref.7
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
64)
|
chain |
B |
residue |
145 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0000269|Ref.7
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
65)
|
chain |
D |
residue |
145 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0000269|Ref.7
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
66)
|
chain |
G |
residue |
145 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0000269|Ref.7
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
67)
|
chain |
A |
residue |
215 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P61983
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
68)
|
chain |
B |
residue |
215 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P61983
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
69)
|
chain |
D |
residue |
215 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P61983
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
70)
|
chain |
G |
residue |
215 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0000250|UniProtKB:P61983
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
71)
|
chain |
A |
residue |
234 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0007744|PubMed:24275569
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
72)
|
chain |
B |
residue |
234 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0007744|PubMed:24275569
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
73)
|
chain |
D |
residue |
234 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0007744|PubMed:24275569
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
74)
|
chain |
G |
residue |
234 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine => ECO:0007744|PubMed:24275569
|
source |
Swiss-Prot : SWS_FT_FI8
|
|
75)
|
chain |
A |
residue |
235 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:24275569
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
76)
|
chain |
B |
residue |
235 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:24275569
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
77)
|
chain |
D |
residue |
235 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:24275569
|
source |
Swiss-Prot : SWS_FT_FI9
|
|
78)
|
chain |
G |
residue |
235 |
type |
MOD_RES |
sequence |
S
|
description |
Phosphoserine => ECO:0007744|PubMed:24275569
|
source |
Swiss-Prot : SWS_FT_FI9
|
|