7OZD
FGFR1 kinase domain (residues 458-765) with mutations C488A, C584S in complex with 34.
This is a non-PDB format compatible entry.
Functional Information from GO Data
Chain | GOid | namespace | contents |
AAA | 0004672 | molecular_function | protein kinase activity |
AAA | 0004713 | molecular_function | protein tyrosine kinase activity |
AAA | 0005007 | molecular_function | fibroblast growth factor receptor activity |
AAA | 0005524 | molecular_function | ATP binding |
AAA | 0006468 | biological_process | protein phosphorylation |
BBB | 0004672 | molecular_function | protein kinase activity |
BBB | 0004713 | molecular_function | protein tyrosine kinase activity |
BBB | 0005007 | molecular_function | fibroblast growth factor receptor activity |
BBB | 0005524 | molecular_function | ATP binding |
BBB | 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. LGEGAFGQVVlAeaigldkdkpnrvtk...VAVK |
Chain | Residue | Details |
AAA | LEU484-LYS514 |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV |
Chain | Residue | Details |
AAA | CYS619-VAL631 |
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:19224897 |
Chain | Residue | Details |
AAA | ASP623 | |
BBB | ASP623 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: |
Chain | Residue | Details |
AAA | LEU484 | |
BBB | ASN568 | |
BBB | ARG627 | |
BBB | ASP641 | |
AAA | LYS514 | |
AAA | GLU562 | |
AAA | ASN568 | |
AAA | ARG627 | |
AAA | ASP641 | |
BBB | LEU484 | |
BBB | LYS514 | |
BBB | GLU562 |
site_id | SWS_FT_FI3 |
Number of Residues | 6 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701 |
Chain | Residue | Details |
AAA | TYR463 | |
AAA | TYR583 | |
AAA | TYR585 | |
BBB | TYR463 | |
BBB | TYR583 | |
BBB | TYR585 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:8622701 |
Chain | Residue | Details |
AAA | TYR653 | |
AAA | TYR654 | |
BBB | TYR653 | |
BBB | TYR654 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:8622701 |
Chain | Residue | Details |
AAA | TYR730 | |
BBB | TYR730 |