Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | BINDING SITE FOR RESIDUE 1LB A 801 |
Chain | Residue |
A | CYS436 |
A | ALA449 |
A | LYS451 |
A | THR493 |
A | GLU494 |
A | MET496 |
A | ASP561 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE NA A 802 |
Chain | Residue |
A | ILE476 |
A | THR478 |
A | HOH929 |
A | GLY471 |
A | HIS473 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGVGSYSVCKrCihkatnme..........FAVK |
Chain | Residue | Details |
A | ILE428-LYS451 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. VvHrDLKpsNILY |
Chain | Residue | Details |
A | VAL535-TYR547 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | ASP539 | |
Chain | Residue | Details |
A | ILE428 | |
A | LYS451 | |
Chain | Residue | Details |
A | SER415 | |
Chain | Residue | Details |
A | TYR529 | |
Chain | Residue | Details |
A | SER556 | |
Chain | Residue | Details |
A | SER715 | |