8XLO
FGFR1 kinase domain with a dual-warhead covalent inhibitor CXF-007
This is a non-PDB format compatible entry.
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 | 0005007 | molecular_function | fibroblast growth factor receptor 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 | 0005007 | molecular_function | fibroblast growth factor receptor 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. LGEGCFGQVVlAeaigldkdkpnrvtk...VAVK |
| Chain | Residue | Details |
| A | LEU484-LYS514 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV |
| Chain | Residue | Details |
| A | 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 |
| A | ASP623 | |
| B | ASP623 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | LEU484 | |
| B | ASN568 | |
| B | ARG627 | |
| B | ASP641 | |
| A | LYS514 | |
| A | GLU562 | |
| A | ASN568 | |
| A | ARG627 | |
| A | ASP641 | |
| B | LEU484 | |
| B | LYS514 | |
| B | 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 |
| A | TYR463 | |
| A | TYR583 | |
| A | TYR585 | |
| B | TYR463 | |
| B | TYR583 | |
| B | 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 |
| A | TYR653 | |
| A | TYR654 | |
| B | TYR653 | |
| B | 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 |
| A | TYR730 | |
| B | TYR730 |
