6XV9
Crystal structure of the kinase domain of human c-KIT in complex with a type-II 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 |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004713 | molecular_function | protein tyrosine kinase activity |
| B | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | binding site for residue O35 A 1001 |
| Chain | Residue |
| A | LEU595 |
| A | GLU671 |
| A | TYR672 |
| A | CYS673 |
| A | GLY676 |
| A | HIS790 |
| A | LEU799 |
| A | ILE808 |
| A | CYS809 |
| A | ASP810 |
| A | PHE811 |
| A | VAL603 |
| A | ALA621 |
| A | LYS623 |
| A | GLU640 |
| A | LEU644 |
| A | ILE653 |
| A | VAL668 |
| A | THR670 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for residue O35 B 1001 |
| Chain | Residue |
| B | VAL603 |
| B | ALA621 |
| B | LYS623 |
| B | GLU640 |
| B | LEU644 |
| B | ILE653 |
| B | VAL654 |
| B | VAL668 |
| B | THR670 |
| B | GLU671 |
| B | TYR672 |
| B | CYS673 |
| B | GLY676 |
| B | CYS788 |
| B | HIS790 |
| B | LEU799 |
| B | ILE808 |
| B | CYS809 |
| B | ASP810 |
| B | PHE811 |
Functional Information from PROSITE/UniProt
| site_id | PS00024 |
| Number of Residues | 16 |
| Details | HEMOPEXIN Hemopexin domain signature. LPvkWmapEsIFNSVY |
| Chain | Residue | Details |
| A | LEU831-TYR846 |
| site_id | PS00107 |
| Number of Residues | 29 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGAFGKVVeAtaqgliksdaamt.....VAVK |
| Chain | Residue | Details |
| A | LEU595-LYS623 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNILL |
| Chain | Residue | Details |
| A | CYS788-LEU800 |
| site_id | PS00240 |
| Number of Residues | 14 |
| Details | RECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GnHeNIVNLLGACT |
| Chain | Residue | Details |
| A | GLY648-THR661 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Region: {"description":"Important for interaction with phosphotyrosine-binding proteins"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| 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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 35 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"12824176","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19265199","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21030588","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9038210","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":"12824176","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9038210","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"10377264","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19265199","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20147452","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"7539802","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"20147452","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"12878163","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"12878163","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20147452","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
