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 | 16 |
Details | BINDING SITE FOR RESIDUE 28D A 801 |
Chain | Residue |
A | ILE428 |
A | SER543 |
A | ASN544 |
A | LEU546 |
A | CYS560 |
A | ASP561 |
A | HOH915 |
A | HOH934 |
A | VAL430 |
A | CYS436 |
A | ALA449 |
A | LYS451 |
A | ILE477 |
A | GLU494 |
A | LEU495 |
A | MET496 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE NA A 802 |
Chain | Residue |
A | GLY471 |
A | HIS473 |
A | ILE476 |
A | THR478 |
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 | ARG538 | |
Chain | Residue | Details |
A | ASP427 | |
A | VAL450 | |
Chain | Residue | Details |
A | ASN414 | |
A | GLN714 | |
Chain | Residue | Details |
A | GLU528 | |
Chain | Residue | Details |
A | GLU555 | |