Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
C | 0004672 | molecular_function | protein kinase activity |
C | 0004674 | molecular_function | protein serine/threonine kinase activity |
C | 0005524 | molecular_function | ATP binding |
C | 0006468 | biological_process | protein phosphorylation |
D | 0004672 | molecular_function | protein kinase activity |
D | 0004674 | molecular_function | protein serine/threonine kinase activity |
D | 0005524 | molecular_function | ATP binding |
D | 0006468 | biological_process | protein phosphorylation |
E | 0004672 | molecular_function | protein kinase activity |
E | 0004674 | molecular_function | protein serine/threonine kinase activity |
E | 0005524 | molecular_function | ATP binding |
E | 0006468 | biological_process | protein phosphorylation |
F | 0004672 | molecular_function | protein kinase activity |
F | 0004674 | molecular_function | protein serine/threonine kinase activity |
F | 0005524 | molecular_function | ATP binding |
F | 0006468 | biological_process | protein phosphorylation |
G | 0004672 | molecular_function | protein kinase activity |
G | 0004674 | molecular_function | protein serine/threonine kinase activity |
G | 0005524 | molecular_function | ATP binding |
G | 0006468 | biological_process | protein phosphorylation |
H | 0004672 | molecular_function | protein kinase activity |
H | 0004674 | molecular_function | protein serine/threonine kinase activity |
H | 0005524 | molecular_function | ATP binding |
H | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | binding site for residue VFA A 501 |
Chain | Residue |
A | ILE98 |
A | VAL153 |
A | MET169 |
A | GLU170 |
A | TYR171 |
A | MET172 |
A | LEU221 |
A | ASP232 |
A | PHE384 |
A | MES502 |
A | GLY101 |
A | ALA102 |
A | PHE103 |
A | GLY104 |
A | VAL106 |
A | ALA119 |
A | LYS121 |
A | LEU123 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue MES A 502 |
Chain | Residue |
A | PHE103 |
A | ASP133 |
A | PHE136 |
A | ARG213 |
A | GLY234 |
A | THR235 |
A | MET237 |
A | VFA501 |
site_id | AC3 |
Number of Residues | 16 |
Details | binding site for residue VFA B 501 |
Chain | Residue |
B | ILE98 |
B | GLY101 |
B | PHE103 |
B | GLY104 |
B | GLU105 |
B | ALA119 |
B | LYS121 |
B | LEU123 |
B | MET169 |
B | GLU170 |
B | TYR171 |
B | MET172 |
B | LEU221 |
B | ALA231 |
B | ASP232 |
B | PHE384 |
site_id | AC4 |
Number of Residues | 2 |
Details | binding site for residue CL B 502 |
Chain | Residue |
B | PHE354 |
B | TRP361 |
site_id | AC5 |
Number of Residues | 19 |
Details | binding site for residue VFA C 501 |
Chain | Residue |
C | ILE98 |
C | GLY101 |
C | PHE103 |
C | GLY104 |
C | GLU105 |
C | VAL106 |
C | ALA119 |
C | LYS121 |
C | LEU123 |
C | MET169 |
C | GLU170 |
C | TYR171 |
C | MET172 |
C | LEU221 |
C | ALA231 |
C | ASP232 |
C | PHE384 |
C | HOH634 |
C | HOH646 |
site_id | AC6 |
Number of Residues | 1 |
Details | binding site for residue CL C 502 |
site_id | AC7 |
Number of Residues | 19 |
Details | binding site for residue VFA D 501 |
Chain | Residue |
D | ILE98 |
D | GLY101 |
D | ALA102 |
D | PHE103 |
D | GLY104 |
D | GLU105 |
D | VAL106 |
D | ALA119 |
D | LYS121 |
D | LEU123 |
D | VAL153 |
D | MET169 |
D | GLU170 |
D | TYR171 |
D | MET172 |
D | LEU221 |
D | ASP232 |
D | PHE384 |
D | MES502 |
site_id | AC8 |
Number of Residues | 6 |
Details | binding site for residue MES D 502 |
Chain | Residue |
D | PHE103 |
D | ASP133 |
D | PHE136 |
D | ARG213 |
D | GLY234 |
D | VFA501 |
site_id | AC9 |
Number of Residues | 17 |
Details | binding site for residue VFA E 501 |
Chain | Residue |
E | TYR171 |
E | MET172 |
E | LEU221 |
E | ASP232 |
E | PHE384 |
E | MES502 |
E | HOH631 |
E | ILE98 |
E | GLY101 |
E | PHE103 |
E | GLY104 |
E | VAL106 |
E | ALA119 |
E | LYS121 |
E | LEU123 |
E | MET169 |
E | GLU170 |
site_id | AD1 |
Number of Residues | 6 |
Details | binding site for residue MES E 502 |
Chain | Residue |
E | PHE103 |
E | ASP133 |
E | PHE136 |
E | ARG213 |
E | GLY234 |
E | VFA501 |
site_id | AD2 |
Number of Residues | 18 |
Details | binding site for residue VFA F 501 |
Chain | Residue |
F | ILE98 |
F | GLY101 |
F | PHE103 |
F | GLY104 |
F | GLU105 |
F | VAL106 |
F | ALA119 |
F | LYS121 |
F | LEU123 |
F | MET169 |
F | GLU170 |
F | TYR171 |
F | MET172 |
F | LEU221 |
F | ALA231 |
F | ASP232 |
F | PHE384 |
F | MES503 |
site_id | AD3 |
Number of Residues | 1 |
Details | binding site for residue CL F 502 |
site_id | AD4 |
Number of Residues | 7 |
Details | binding site for residue MES F 503 |
Chain | Residue |
F | PHE103 |
F | ASP133 |
F | PHE136 |
F | ARG213 |
F | GLY234 |
F | VAL251 |
F | VFA501 |
site_id | AD5 |
Number of Residues | 16 |
Details | binding site for residue VFA G 501 |
Chain | Residue |
G | ILE98 |
G | GLY101 |
G | PHE103 |
G | GLY104 |
G | VAL106 |
G | ALA119 |
G | LYS121 |
G | LEU123 |
G | MET169 |
G | GLU170 |
G | TYR171 |
G | MET172 |
G | LEU221 |
G | ASP232 |
G | PHE384 |
G | MES502 |
site_id | AD6 |
Number of Residues | 6 |
Details | binding site for residue MES G 502 |
Chain | Residue |
G | PHE103 |
G | ASP133 |
G | PHE136 |
G | ARG213 |
G | GLY234 |
G | VFA501 |
site_id | AD7 |
Number of Residues | 20 |
Details | binding site for residue VFA H 501 |
Chain | Residue |
H | ILE98 |
H | GLY101 |
H | ALA102 |
H | PHE103 |
H | GLY104 |
H | GLU105 |
H | VAL106 |
H | ALA119 |
H | LYS121 |
H | LEU123 |
H | MET169 |
H | GLU170 |
H | TYR171 |
H | MET172 |
H | LEU221 |
H | ALA231 |
H | ASP232 |
H | PHE384 |
H | MES502 |
H | HOH627 |
site_id | AD8 |
Number of Residues | 10 |
Details | binding site for residue MES H 502 |
Chain | Residue |
H | ASP133 |
H | PHE136 |
H | ARG213 |
H | GLY234 |
H | THR235 |
H | MET237 |
H | THR249 |
H | VAL251 |
H | VFA501 |
H | HOH615 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGAFGEVQlVrhkasqkv..........YAMK |
Chain | Residue | Details |
A | ILE98-LYS121 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiHrDVKpdNMLL |
Chain | Residue | Details |
A | LEU210-LEU222 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP214 | |
B | ASP214 | |
C | ASP214 | |
D | ASP214 | |
E | ASP214 | |
F | ASP214 | |
G | ASP214 | |
H | ASP214 | |
Chain | Residue | Details |
E | ILE98 | |
E | LYS121 | |
F | ILE98 | |
F | LYS121 | |
G | ILE98 | |
G | LYS121 | |
H | ILE98 | |
H | LYS121 | |
A | LYS121 | |
B | ILE98 | |
B | LYS121 | |
C | ILE98 | |
C | LYS121 | |
D | ILE98 | |
D | LYS121 | |
A | ILE98 | |
Chain | Residue | Details |
B | THR414 | |
C | THR414 | |
D | THR414 | |
E | THR414 | |
F | THR414 | |
G | THR414 | |
H | THR414 | |
A | THR414 | |