2PVF
Crystal Structure of Tyrosine Phosphorylated Activated FGF Receptor 2 (FGFR2) Kinase Domain in Complex with ATP Analog and Substrate Peptide
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 301 |
| Chain | Residue |
| A | HOH2 |
| A | ACP300 |
| A | ASN631 |
| A | ASP644 |
| B | HOH1 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 302 |
| Chain | Residue |
| A | ACP300 |
| A | HOH111 |
| A | HOH112 |
| A | HOH113 |
| A | HOH114 |
| site_id | AC3 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE ACP A 300 |
| Chain | Residue |
| A | HOH57 |
| A | HOH76 |
| A | HOH112 |
| A | MG301 |
| A | MG302 |
| A | LEU487 |
| A | GLY488 |
| A | GLY490 |
| A | ALA491 |
| A | PHE492 |
| A | GLY493 |
| A | VAL495 |
| A | ALA515 |
| A | LYS517 |
| A | VAL564 |
| A | GLU565 |
| A | ALA567 |
| A | ASN571 |
| A | ARG630 |
| A | ASN631 |
| A | LEU633 |
| A | ASP644 |
| B | HOH1 |
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 | LEU487-LYS517 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNVLV |
| Chain | Residue | Details |
| A | CYS622-VAL634 |
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 | 3 |
| 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 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"15629145","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19060208","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 | ASP626 | |
| A | ARG630 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP626 | |
| A | ALA628 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR661 | |
| A | ASP626 | |
| A | ALA628 |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP626 | |
| A | ALA628 | |
| A | ASN631 |
