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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 18 |
Details | binding site for residue B4V A 501 |
Chain | Residue |
A | ILE82 |
A | ASP117 |
A | PHE120 |
A | VAL137 |
A | GLU154 |
A | TYR155 |
A | MET156 |
A | LEU205 |
A | GLY218 |
A | PHE368 |
A | GLY85 |
A | ALA86 |
A | PHE87 |
A | GLY88 |
A | GLU89 |
A | VAL90 |
A | ALA103 |
A | LEU107 |
site_id | AC2 |
Number of Residues | 5 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
A | ASP169 |
A | VAL170 |
A | MET271 |
A | LEU272 |
A | ASP304 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | ASN163 |
A | SER166 |
A | ASN167 |
A | ASP369 |
C | GLU12 |
site_id | AC4 |
Number of Residues | 17 |
Details | binding site for residue B4V B 900 |
Chain | Residue |
B | GLY85 |
B | ALA86 |
B | PHE87 |
B | GLY88 |
B | GLU89 |
B | VAL90 |
B | ALA103 |
B | LEU107 |
B | ASP117 |
B | PHE120 |
B | VAL137 |
B | MET153 |
B | GLU154 |
B | TYR155 |
B | MET156 |
B | LEU205 |
B | GLY218 |
site_id | AC5 |
Number of Residues | 19 |
Details | binding site for residue B4V C 900 |
Chain | Residue |
C | ILE82 |
C | GLY85 |
C | ALA86 |
C | PHE87 |
C | GLY88 |
C | VAL90 |
C | ALA103 |
C | LEU107 |
C | ASP117 |
C | PHE120 |
C | VAL137 |
C | MET153 |
C | GLU154 |
C | TYR155 |
C | MET156 |
C | LEU205 |
C | ASP216 |
C | PHE368 |
C | HOH1009 |
site_id | AC6 |
Number of Residues | 18 |
Details | binding site for residue B4V D 900 |
Chain | Residue |
A | ASP281 |
D | ILE82 |
D | GLY85 |
D | ALA86 |
D | PHE87 |
D | VAL90 |
D | ALA103 |
D | ASP117 |
D | PHE120 |
D | VAL137 |
D | GLU154 |
D | TYR155 |
D | MET156 |
D | LEU205 |
D | PHE368 |
D | HOH1011 |
D | HOH1021 |
D | HOH1028 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGAFGEVQlVrhkstrkv..........YAMK |
Chain | Residue | Details |
A | ILE82-LYS105 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. FiHrDVKpdNMLL |
Chain | Residue | Details |
A | PHE194-LEU206 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP198 | |
B | ASP198 | |
C | ASP198 | |
D | ASP198 | |
Chain | Residue | Details |
A | ILE82 | |
A | LYS105 | |
B | ILE82 | |
B | LYS105 | |
C | ILE82 | |
C | LYS105 | |
D | ILE82 | |
D | LYS105 | |