|
|
1)
|
chain |
H |
residue |
31 |
type |
|
sequence |
D
|
description |
binding site for residue GOL H 301
|
source |
: AC1
|
|
2)
|
chain |
H |
residue |
32 |
type |
|
sequence |
Y
|
description |
binding site for residue GOL H 301
|
source |
: AC1
|
|
3)
|
chain |
H |
residue |
53 |
type |
|
sequence |
Q
|
description |
binding site for residue GOL H 301
|
source |
: AC1
|
|
4)
|
chain |
H |
residue |
100 |
type |
|
sequence |
F
|
description |
binding site for residue GOL H 301
|
source |
: AC1
|
|
5)
|
chain |
H |
residue |
100 |
type |
|
sequence |
F
|
description |
binding site for residue GOL H 301
|
source |
: AC1
|
|
6)
|
chain |
H |
residue |
101 |
type |
|
sequence |
V
|
description |
binding site for residue GOL H 301
|
source |
: AC1
|
|
7)
|
chain |
H |
residue |
101 |
type |
|
sequence |
V
|
description |
binding site for residue GOL H 301
|
source |
: AC1
|
|
8)
|
chain |
H |
residue |
102 |
type |
|
sequence |
R
|
description |
binding site for residue GOL H 301
|
source |
: AC1
|
|
9)
|
chain |
H |
residue |
106 |
type |
|
sequence |
W
|
description |
binding site for residue GOL H 301
|
source |
: AC1
|
|
10)
|
chain |
H |
residue |
104 |
type |
|
sequence |
F
|
description |
binding site for residue GOL H 302
|
source |
: AC2
|
|
11)
|
chain |
H |
residue |
106 |
type |
|
sequence |
W
|
description |
binding site for residue GOL H 302
|
source |
: AC2
|
|
12)
|
chain |
H |
residue |
106 |
type |
|
sequence |
W
|
description |
binding site for residue GOL H 302
|
source |
: AC2
|
|
13)
|
chain |
P |
residue |
4 |
type |
|
sequence |
X
|
description |
binding site for residue GOL H 302
|
source |
: AC2
|
|
14)
|
chain |
P |
residue |
6 |
type |
|
sequence |
T
|
description |
binding site for residue GOL H 302
|
source |
: AC2
|
|
15)
|
chain |
H |
residue |
30 |
type |
|
sequence |
R
|
description |
binding site for residue GOL H 303
|
source |
: AC3
|
|
16)
|
chain |
H |
residue |
73 |
type |
|
sequence |
D
|
description |
binding site for residue GOL H 303
|
source |
: AC3
|
|
17)
|
chain |
H |
residue |
74 |
type |
|
sequence |
N
|
description |
binding site for residue GOL H 303
|
source |
: AC3
|
|
18)
|
chain |
H |
residue |
75 |
type |
|
sequence |
A
|
description |
binding site for residue GOL H 303
|
source |
: AC3
|
|
19)
|
chain |
H |
residue |
27 |
type |
|
sequence |
F
|
description |
binding site for residue GOL H 304
|
source |
: AC4
|
|
20)
|
chain |
H |
residue |
98 |
type |
|
sequence |
R
|
description |
binding site for residue GOL H 304
|
source |
: AC4
|
|
21)
|
chain |
H |
residue |
16 |
type |
|
sequence |
R
|
description |
binding site for residue GOL H 305
|
source |
: AC5
|
|
22)
|
chain |
H |
residue |
17 |
type |
|
sequence |
S
|
description |
binding site for residue GOL H 305
|
source |
: AC5
|
|
23)
|
chain |
L |
residue |
36 |
type |
|
sequence |
Q
|
description |
binding site for residue GOL L 301
|
source |
: AC6
|
|
24)
|
chain |
L |
residue |
38 |
type |
|
sequence |
R
|
description |
binding site for residue GOL L 301
|
source |
: AC6
|
|
25)
|
chain |
L |
residue |
57 |
type |
|
sequence |
I
|
description |
binding site for residue GOL L 301
|
source |
: AC6
|
|
26)
|
chain |
L |
residue |
58 |
type |
|
sequence |
P
|
description |
binding site for residue GOL L 301
|
source |
: AC6
|
|
27)
|
chain |
L |
residue |
61 |
type |
|
sequence |
F
|
description |
binding site for residue GOL L 301
|
source |
: AC6
|
|
28)
|
chain |
L |
residue |
80 |
type |
|
sequence |
G
|
description |
binding site for residue GOL L 301
|
source |
: AC6
|
|
29)
|
chain |
L |
residue |
81 |
type |
|
sequence |
D
|
description |
binding site for residue GOL L 301
|
source |
: AC6
|
|
30)
|
chain |
L |
residue |
58 |
type |
|
sequence |
P
|
description |
binding site for residue GOL L 302
|
source |
: AC7
|
|
31)
|
chain |
L |
residue |
59 |
type |
|
sequence |
E
|
description |
binding site for residue GOL L 302
|
source |
: AC7
|
|
32)
|
chain |
L |
residue |
60 |
type |
|
sequence |
R
|
description |
binding site for residue GOL L 302
|
source |
: AC7
|
|
33)
|
chain |
L |
residue |
76 |
type |
|
sequence |
R
|
description |
binding site for residue GOL L 302
|
source |
: AC7
|
|
34)
|
chain |
L |
residue |
67 |
type |
|
sequence |
G
|
description |
binding site for residue SO4 L 303
|
source |
: AC8
|
|
35)
|
chain |
L |
residue |
68 |
type |
|
sequence |
N
|
description |
binding site for residue SO4 L 303
|
source |
: AC8
|
|
36)
|
chain |
L |
residue |
69 |
type |
|
sequence |
T
|
description |
binding site for residue SO4 L 303
|
source |
: AC8
|
|
37)
|
chain |
H |
residue |
33 |
type |
|
sequence |
W
|
description |
binding site for Ligand residues M3L P 4 through GLN P 5 bound to THR P 3
|
source |
: AC9
|
|
38)
|
chain |
H |
residue |
50 |
type |
|
sequence |
D
|
description |
binding site for Ligand residues M3L P 4 through GLN P 5 bound to THR P 3
|
source |
: AC9
|
|
39)
|
chain |
H |
residue |
103 |
type |
|
sequence |
G
|
description |
binding site for Ligand residues M3L P 4 through GLN P 5 bound to THR P 3
|
source |
: AC9
|
|
40)
|
chain |
H |
residue |
106 |
type |
|
sequence |
W
|
description |
binding site for Ligand residues M3L P 4 through GLN P 5 bound to THR P 3
|
source |
: AC9
|
|
41)
|
chain |
L |
residue |
29 |
type |
|
sequence |
D
|
description |
binding site for Ligand residues M3L P 4 through GLN P 5 bound to THR P 3
|
source |
: AC9
|
|
42)
|
chain |
L |
residue |
90 |
type |
|
sequence |
W
|
description |
binding site for Ligand residues M3L P 4 through GLN P 5 bound to THR P 3
|
source |
: AC9
|
|
43)
|
chain |
L |
residue |
97 |
type |
|
sequence |
Y
|
description |
binding site for Ligand residues M3L P 4 through GLN P 5 bound to THR P 3
|
source |
: AC9
|
|
44)
|
chain |
P |
residue |
3 |
type |
|
sequence |
T
|
description |
binding site for Ligand residues M3L P 4 through GLN P 5 bound to THR P 3
|
source |
: AC9
|
|
45)
|
chain |
P |
residue |
6 |
type |
|
sequence |
T
|
description |
binding site for Ligand residues M3L P 4 through GLN P 5 bound to THR P 3
|
source |
: AC9
|
|
46)
|
chain |
P |
residue |
6 |
type |
|
sequence |
T
|
description |
binding site for Ligand residues M3L P 4 through GLN P 5 bound to THR P 3
|
source |
: AC9
|
|
47)
|
chain |
P |
residue |
7 |
type |
|
sequence |
A
|
description |
binding site for Ligand residues M3L P 4 through GLN P 5 bound to THR P 3
|
source |
: AC9
|
|
48)
|
chain |
P |
residue |
2 |
type |
MOD_RES |
sequence |
R
|
description |
Citrulline; alternate => ECO:0000269|PubMed:16567635
|
source |
Swiss-Prot : SWS_FT_FI1
|
|
49)
|
chain |
L |
residue |
14-25 |
type |
prosite |
sequence |
PGQTARITCGGT
|
description |
AA_TRNA_LIGASE_I Aminoacyl-transfer RNA synthetases class-I signature. PgqTArITCGGT
|
source |
prosite : PS00178
|
|
50)
|
chain |
P |
residue |
3 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine; by HASPIN => ECO:0000269|PubMed:15681610, ECO:0000269|PubMed:16185088
|
source |
Swiss-Prot : SWS_FT_FI2
|
|
51)
|
chain |
P |
residue |
4 |
type |
MOD_RES |
sequence |
X
|
description |
N6-methyllysine; alternate => ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
|
source |
Swiss-Prot : SWS_FT_FI3
|
|
52)
|
chain |
P |
residue |
5 |
type |
MOD_RES |
sequence |
Q
|
description |
5-glutamyl serotonin; alternate => ECO:0000269|PubMed:30867594
|
source |
Swiss-Prot : SWS_FT_FI4
|
|
53)
|
chain |
P |
residue |
6 |
type |
MOD_RES |
sequence |
T
|
description |
Phosphothreonine; by PKC => ECO:0000269|PubMed:20228790
|
source |
Swiss-Prot : SWS_FT_FI5
|
|
54)
|
chain |
P |
residue |
8 |
type |
MOD_RES |
sequence |
R
|
description |
Symmetric dimethylarginine; by PRMT5; alternate => ECO:0000250|UniProtKB:P68433
|
source |
Swiss-Prot : SWS_FT_FI6
|
|
55)
|
chain |
P |
residue |
9 |
type |
MOD_RES |
sequence |
K
|
description |
N6-methyllysine; alternate => ECO:0000269|PubMed:11242053, ECO:0000269|PubMed:16185088, ECO:0000269|PubMed:16267050, ECO:0000269|PubMed:16457588, ECO:0000269|PubMed:17194708
|
source |
Swiss-Prot : SWS_FT_FI7
|
|
56)
|
chain |
H |
residue |
202-208 |
type |
prosite |
sequence |
YICNVNH
|
description |
IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
|
source |
prosite : PS00290
|
|
57)
|
chain |
L |
residue |
193-199 |
type |
prosite |
sequence |
YACEVTH
|
description |
IG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YICNVNH
|
source |
prosite : PS00290
|
|