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 | 14 |
Details | binding site for residue MU7 A 501 |
Chain | Residue |
A | ILE227 |
A | PHE356 |
A | GLY367 |
A | ASP368 |
A | LEU369 |
A | HOH781 |
A | LYS233 |
A | VAL235 |
A | VAL281 |
A | THR301 |
A | LEU303 |
A | MET304 |
A | THR305 |
A | GLY307 |
site_id | AC2 |
Number of Residues | 8 |
Details | binding site for residue GOL A 502 |
Chain | Residue |
A | PRO392 |
A | TYR422 |
A | ARG434 |
A | VAL435 |
A | GLY438 |
A | VAL439 |
A | ILE460 |
A | GLN462 |
site_id | AC3 |
Number of Residues | 8 |
Details | binding site for residue GOL A 503 |
Chain | Residue |
A | ALA382 |
A | VAL383 |
A | ILE384 |
A | GLY385 |
A | PRO387 |
A | ASN427 |
A | ALA428 |
A | HOH664 |
site_id | AC4 |
Number of Residues | 3 |
Details | binding site for residue GOL A 504 |
Chain | Residue |
A | GLU424 |
A | ARG434 |
A | ALA442 |
site_id | AC5 |
Number of Residues | 2 |
Details | binding site for residue GOL A 505 |
Chain | Residue |
A | TYR432 |
A | THR436 |
site_id | AC6 |
Number of Residues | 2 |
Details | binding site for residue ACT A 506 |
Chain | Residue |
A | ASP203 |
A | ACT507 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue ACT A 507 |
Chain | Residue |
A | THR244 |
A | ACT506 |
A | HOH616 |
A | HOH721 |
site_id | AC8 |
Number of Residues | 3 |
Details | binding site for residue ACT A 508 |
Chain | Residue |
A | MET319 |
A | ALA416 |
A | HOH654 |
Functional Information from PROSITE/UniProt
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKcdNIFI |
Chain | Residue | Details |
A | ILE345-ILE357 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 258 |
Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"10828064","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16083423","evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 5 |
Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9H4A3","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"24803536","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4Q2A","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"12374799","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"12374799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22544747","evidenceCode":"ECO:0000269"}]} |