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 | 15 |
Details | binding site for residue B4J A 501 |
Chain | Residue |
A | ILE82 |
A | MET153 |
A | GLU154 |
A | LEU205 |
A | ASP216 |
A | GLY218 |
A | HOH602 |
A | GLY85 |
A | ALA86 |
A | PHE87 |
A | VAL90 |
A | LYS105 |
A | LEU107 |
A | ASP117 |
A | PHE120 |
site_id | AC2 |
Number of Residues | 3 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
A | GLU270 |
A | GLY274 |
A | HOH611 |
site_id | AC3 |
Number of Residues | 14 |
Details | binding site for residue B4J B 900 |
Chain | Residue |
B | GLY85 |
B | ALA86 |
B | PHE87 |
B | VAL90 |
B | ALA103 |
B | LYS105 |
B | ASP117 |
B | PHE120 |
B | GLU154 |
B | LEU205 |
B | ALA215 |
B | ASP216 |
B | GLY218 |
B | PHE368 |
site_id | AC4 |
Number of Residues | 16 |
Details | binding site for residue B4J C 900 |
Chain | Residue |
C | ILE82 |
C | GLY85 |
C | ALA86 |
C | PHE87 |
C | GLY88 |
C | VAL90 |
C | LYS105 |
C | LEU107 |
C | ASP117 |
C | PHE120 |
C | MET153 |
C | GLU154 |
C | LEU205 |
C | ASP216 |
C | GLY218 |
C | HOH1002 |
site_id | AC5 |
Number of Residues | 15 |
Details | binding site for residue B4J D 900 |
Chain | Residue |
D | GLY85 |
D | ALA86 |
D | PHE87 |
D | VAL90 |
D | LYS105 |
D | ASP117 |
D | PHE120 |
D | VAL137 |
D | MET153 |
D | GLU154 |
D | LEU205 |
D | ASP216 |
D | GLY218 |
D | PHE368 |
D | HOH1002 |
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 |
B | ASP198 | |
C | ASP198 | |
D | ASP198 | |
A | ASP198 | |
Chain | Residue | Details |
C | ILE82 | |
C | LYS105 | |
D | ILE82 | |
D | LYS105 | |
A | ILE82 | |
A | LYS105 | |
B | ILE82 | |
B | LYS105 | |