4ZSA
Crystal structure of FGFR1 kinase domain in complex with 7n
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 PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue 4UT A 801 |
| Chain | Residue |
| A | LEU484 |
| A | ALA564 |
| A | SER565 |
| A | GLY567 |
| A | LEU630 |
| A | GLY485 |
| A | PHE489 |
| A | ALA512 |
| A | LYS514 |
| A | GLU531 |
| A | VAL561 |
| A | GLU562 |
| A | TYR563 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | binding site for residue 4UT B 801 |
| Chain | Residue |
| B | PHE489 |
| B | ALA512 |
| B | LYS514 |
| B | GLU531 |
| B | VAL561 |
| B | GLU562 |
| B | TYR563 |
| B | ALA564 |
| B | SER565 |
| B | GLY567 |
| B | GLU571 |
| B | LEU630 |
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 |
| 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 | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19224897","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 24 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16507368","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19224897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19665973","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8622701","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"19224897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8622701","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16507368","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19224897","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"8622701","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
