2PVY
Crystal Structure of FGF Receptor 2 (FGFR2) Kinase Domain Harboring the Pathogenic K659N Mutation Responsible for an Unclassified Craniosynostosis Syndrome.
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 | 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 | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004713 | molecular_function | protein tyrosine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004713 | molecular_function | protein tyrosine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 A 801 |
| Chain | Residue |
| A | ARG625 |
| A | ARG649 |
| A | TYR657 |
| A | THR660 |
| site_id | AC2 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACP A 802 |
| Chain | Residue |
| A | ASN571 |
| A | LEU633 |
| A | HOH932 |
| A | HOH950 |
| A | HOH956 |
| A | LEU487 |
| A | ALA515 |
| A | VAL564 |
| A | GLU565 |
| A | ALA567 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 8001 |
| Chain | Residue |
| B | ARG625 |
| B | ARG649 |
| B | TYR657 |
| B | ARG664 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE ACP B 8002 |
| Chain | Residue |
| B | LEU487 |
| B | VAL495 |
| B | ALA515 |
| B | VAL564 |
| B | GLU565 |
| B | TYR566 |
| B | ALA567 |
| B | ASN571 |
| B | ARG630 |
| B | LEU633 |
| B | ASP644 |
| B | HOH9041 |
| B | HOH9047 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE SO4 C 801 |
| Chain | Residue |
| C | ARG625 |
| C | ARG649 |
| C | TYR657 |
| C | ARG664 |
| C | HOH918 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE ACP C 802 |
| Chain | Residue |
| C | LEU487 |
| C | ALA515 |
| C | VAL564 |
| C | GLU565 |
| C | TYR566 |
| C | ALA567 |
| C | ASN571 |
| C | LEU633 |
| C | HOH938 |
| site_id | AC7 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 801 |
| Chain | Residue |
| D | ARG625 |
| D | ARG649 |
| D | TYR657 |
| D | THR660 |
| D | ARG664 |
| D | HOH954 |
| site_id | AC8 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ACP D 802 |
| Chain | Residue |
| D | LEU487 |
| D | ALA515 |
| D | VAL564 |
| D | GLU565 |
| D | TYR566 |
| D | ALA567 |
| D | ASN571 |
| D | LEU633 |
| D | HOH956 |
| D | HOH957 |
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 | 4 |
| 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 | 16 |
| 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 | 8 |
| 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 | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"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 | ASP626 | |
| A | ARG630 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | THR661 | |
| D | ASP626 | |
| D | ALA628 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP626 | |
| A | ALA628 | |
| A | ASN631 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP626 | |
| B | ALA628 | |
| B | ASN631 |
| site_id | CSA13 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP626 | |
| C | ALA628 | |
| C | ASN631 |
| site_id | CSA14 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP626 | |
| D | ALA628 | |
| D | ASN631 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP626 | |
| B | ARG630 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP626 | |
| C | ARG630 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP626 | |
| D | ARG630 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP626 | |
| A | ALA628 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP626 | |
| B | ALA628 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| C | ASP626 | |
| C | ALA628 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| D | ASP626 | |
| D | ALA628 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR661 | |
| A | ASP626 | |
| A | ALA628 |
