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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE M77 A 418 |
Chain | Residue |
A | ILE82 |
A | LEU207 |
A | PHE370 |
A | GLY83 |
A | VAL90 |
A | ALA103 |
A | ASP154 |
A | TYR155 |
A | TYR156 |
A | ASP204 |
A | ASN205 |
site_id | AC2 |
Number of Residues | 2 |
Details | BINDING SITE FOR RESIDUE M77 A 419 |
Chain | Residue |
A | HOH488 |
A | HOH519 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 420 |
Chain | Residue |
A | PHE87 |
A | LYS105 |
A | LEU107 |
A | CYS120 |
A | GLU124 |
A | GLY220 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR RESIDUE M77 B 418 |
Chain | Residue |
B | ILE82 |
B | GLY83 |
B | ARG84 |
B | VAL90 |
B | ALA103 |
B | ASP154 |
B | TYR155 |
B | TYR156 |
B | ASP204 |
B | ASN205 |
B | LEU207 |
B | PHE370 |
site_id | AC5 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE M77 B 419 |
site_id | AC6 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO B 420 |
Chain | Residue |
B | PHE87 |
B | LYS105 |
B | LEU107 |
B | GLU124 |
B | ASP218 |
B | GLY220 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGRGAFGEVAvVkmknteri..........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. YvHrDIKpdNVLL |
Chain | Residue | Details |
A | TYR196-LEU208 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP200 | |
B | ASP200 | |
Chain | Residue | Details |
A | ILE82 | |
B | ILE82 | |
Chain | Residue | Details |
A | LYS105 | |
B | LYS105 | |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000250 |
Chain | Residue | Details |
A | SER221 | |
A | SER233 | |
B | SER221 | |
B | SER233 | |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250 |
Chain | Residue | Details |
A | THR239 | |
B | THR239 | |