3EWH
Crystal structure of the VEGFR2 kinase domain in complex with a pyridyl-pyrimidine benzimidazole inhibitor
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 | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 16 |
| Details | BINDING SITE FOR RESIDUE K11 A 1 |
| Chain | Residue |
| A | HOH77 |
| A | GLU917 |
| A | PHE918 |
| A | CYS919 |
| A | LEU1019 |
| A | HIS1026 |
| A | ASP1046 |
| A | PHE1047 |
| A | LEU840 |
| A | VAL848 |
| A | ALA866 |
| A | LYS868 |
| A | GLU885 |
| A | ILE892 |
| A | VAL898 |
| A | THR916 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE EDO A2762 |
| Chain | Residue |
| A | HOH32 |
| A | HOH301 |
| A | SER1100 |
| A | PRO1128 |
| A | ASP1129 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 29 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGAFGQVIeAdafgidktatcrt.....VAVK |
| Chain | Residue | Details |
| A | LEU840-LYS868 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNILL |
| Chain | Residue | Details |
| A | CYS1024-LEU1036 |
| site_id | PS00240 |
| Number of Residues | 14 |
| Details | RECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GhHlNVVNLLGACT |
| Chain | Residue | Details |
| A | GLY893-THR906 |
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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"10102632","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18936167","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":"10037737","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10102632","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10368301","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15215251","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15962004","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18936167","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 | ASP1028 | |
| A | ARG1032 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ALA1030 | |
| A | ASP1028 |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ALA1030 | |
| A | ASP1028 | |
| A | ASN1033 |
