3CLY
Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domains Trapped in Trans-Phosphorylation Reaction
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 1801 |
| Chain | Residue |
| A | ASN1631 |
| A | ASP1644 |
| A | ACP1803 |
| A | HOH1901 |
| A | HOH1902 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE MG A 1802 |
| Chain | Residue |
| A | GLU1534 |
| A | ASP1644 |
| A | GLY1646 |
| A | ACP1803 |
| site_id | AC3 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE ACP A 1803 |
| Chain | Residue |
| A | LEU1487 |
| A | GLY1488 |
| A | GLN1494 |
| A | VAL1495 |
| A | ALA1515 |
| A | LYS1517 |
| A | VAL1564 |
| A | GLU1565 |
| A | ALA1567 |
| A | ASN1571 |
| A | ARG1630 |
| A | ASN1631 |
| A | LEU1633 |
| A | ASP1644 |
| A | MG1801 |
| A | MG1802 |
| A | HOH1901 |
| A | HOH1912 |
| A | HOH1916 |
| A | HOH1922 |
| A | HOH1939 |
| A | HOH1978 |
| A | HOH1985 |
| A | HOH1986 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 31 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGEGAFGQVVmAeavgidkdkpkeavt...VAVK |
| Chain | Residue | Details |
| A | LEU1487-LYS1517 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV |
| Chain | Residue | Details |
| A | CYS1622-VAL1634 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| 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":"19060208","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"17803937","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19060208","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19410646","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 | ARG1630 | |
| A | ASP1626 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ALA1628 | |
| A | ASP1626 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ALA1628 | |
| A | THR1661 | |
| A | ASP1626 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN1631 | |
| A | ALA1628 | |
| A | ASP1626 |
