Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004712 | molecular_function | protein serine/threonine/tyrosine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
A | 0046777 | biological_process | protein autophosphorylation |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 7 |
Details | binding site for residue SO4 A 501 |
Chain | Residue |
A | SER169 |
A | LYS193 |
A | LYS194 |
A | HOH689 |
A | HOH778 |
A | HOH842 |
A | HOH916 |
site_id | AC2 |
Number of Residues | 7 |
Details | binding site for residue SO4 A 502 |
Chain | Residue |
A | ARG328 |
A | GLU366 |
A | HOH631 |
A | HOH906 |
A | HOH928 |
A | ASN232 |
A | ARG325 |
site_id | AC3 |
Number of Residues | 4 |
Details | binding site for residue SO4 A 503 |
Chain | Residue |
A | LYS264 |
A | ARG300 |
A | SER301 |
A | HOH851 |
site_id | AC4 |
Number of Residues | 8 |
Details | binding site for residue KQZ A 504 |
Chain | Residue |
A | PHE170 |
A | ALA186 |
A | LYS188 |
A | PHE238 |
A | GLU239 |
A | LEU241 |
A | LEU294 |
A | EDO506 |
site_id | AC5 |
Number of Residues | 11 |
Details | binding site for residue EDO A 505 |
Chain | Residue |
A | ASN198 |
A | GLN199 |
A | GLN199 |
A | ILE202 |
A | ILE202 |
A | TYR319 |
A | TYR319 |
A | HOH633 |
A | HOH633 |
A | HOH655 |
A | HOH655 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EDO A 506 |
Chain | Residue |
A | GLY166 |
A | ASN244 |
A | KQZ504 |
A | HOH622 |
A | HOH648 |
A | HOH751 |
A | HOH781 |
site_id | AC7 |
Number of Residues | 7 |
Details | binding site for residue EDO A 507 |
Chain | Residue |
A | TYR243 |
A | ASN251 |
A | LEU274 |
A | HOH625 |
A | HOH755 |
A | HOH821 |
A | HOH853 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGKGSFGQVVkAydrveqew..........VAIK |
Chain | Residue | Details |
A | ILE165-LYS188 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHcDLKpeNILL |
Chain | Residue | Details |
A | ILE283-LEU295 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 1 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19690332","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q63470","evidenceCode":"ECO:0000250"}]} |
site_id | SWS_FT_FI6 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI7 |
Number of Residues | 1 |
Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"23665168","evidenceCode":"ECO:0000269"}]} |