2FGI
CRYSTAL STRUCTURE OF THE TYROSINE KINASE DOMAIN OF FGF RECEPTOR 1 IN COMPLEX WITH INHIBITOR PD173074
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 | 16 |
| Details | BINDING SITE FOR RESIDUE PD1 B 1000 |
| Chain | Residue |
| B | LEU484 |
| B | GLU562 |
| B | TYR563 |
| B | ALA564 |
| B | SER565 |
| B | GLU571 |
| B | LEU630 |
| B | ASP641 |
| B | GLY485 |
| B | GLU486 |
| B | VAL492 |
| B | LYS514 |
| B | GLU531 |
| B | ILE545 |
| B | VAL559 |
| B | VAL561 |
| site_id | AC2 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE PD1 A 1001 |
| Chain | Residue |
| A | HOH30 |
| A | LEU484 |
| A | GLY485 |
| A | VAL492 |
| A | LYS514 |
| A | MET535 |
| A | ILE545 |
| A | VAL559 |
| A | VAL561 |
| A | GLU562 |
| A | TYR563 |
| A | ALA564 |
| A | SER565 |
| A | GLY567 |
| A | LEU630 |
| A | ALA640 |
| A | ASP641 |
| A | PHE642 |
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 | 18 |
| 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 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ARG627 | |
| A | ASP623 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ARG627 | |
| B | ASP623 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ALA625 | |
| A | ASP623 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ALA625 | |
| B | ASP623 |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN628 | |
| A | ALA625 | |
| A | ASP623 |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN628 | |
| B | ALA625 | |
| B | ASP623 |
