7KIA
Crystal structure of FGFR2 kinase domain gatekeeper mutant V564F in complex with covalent compound 19
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004713 | molecular_function | protein tyrosine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004713 | molecular_function | protein tyrosine kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 31 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGCFGQVVmAeavgidkdkpkeavt...VAVK |
Chain | Residue | Details |
A | LEU487-LYS517 |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV |
Chain | Residue | Details |
A | CYS622-VAL634 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028, ECO:0000269|PubMed:19060208 |
Chain | Residue | Details |
A | ASP626 | |
B | ASP626 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:19060208 |
Chain | Residue | Details |
A | LEU487 | |
A | LYS517 | |
A | GLU565 | |
A | ASN571 | |
B | LEU487 | |
B | LYS517 | |
B | GLU565 | |
B | ASN571 |
site_id | SWS_FT_FI3 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646 |
Chain | Residue | Details |
A | TYR466 | |
A | TYR588 | |
B | TYR466 | |
B | TYR588 |
site_id | SWS_FT_FI4 |
Number of Residues | 6 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646 |
Chain | Residue | Details |
A | TYR586 | |
A | TYR656 | |
A | TYR657 | |
B | TYR586 | |
B | TYR656 | |
B | TYR657 |