8PQA
c-KIT kinase domain in complex with avapritinib derivative 4
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 |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004713 | molecular_function | protein tyrosine kinase activity |
| C | 0004714 | molecular_function | transmembrane receptor protein tyrosine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 0007169 | biological_process | cell surface receptor protein tyrosine kinase signaling pathway |
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 | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028 |
| Chain | Residue | Details |
| A | ASP792 | |
| C | ASP792 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | TYR568 | |
| A | GLY596 | |
| A | LYS623 | |
| A | GLU671 | |
| A | ARG796 | |
| A | ASN797 | |
| A | ASP810 | |
| C | TYR568 | |
| C | GLY596 | |
| C | LYS623 | |
| C | GLU671 | |
| C | ARG796 | |
| C | ASN797 | |
| C | ASP810 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:20147452 |
| Chain | Residue | Details |
| A | TYR553 | |
| C | TYR553 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:19265199, ECO:0000269|PubMed:21030588, ECO:0000269|PubMed:9038210 |
| Chain | Residue | Details |
| A | TYR568 | |
| C | TYR568 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12824176, ECO:0000269|PubMed:9038210 |
| Chain | Residue | Details |
| A | TYR570 | |
| C | TYR570 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:7539802 |
| Chain | Residue | Details |
| A | SER821 | |
| C | SER821 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:20147452 |
| Chain | Residue | Details |
| A | TYR823 | |
| C | TYR823 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:12878163 |
| Chain | Residue | Details |
| A | SER891 | |
| C | SER891 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:12878163, ECO:0000269|PubMed:20147452 |
| Chain | Residue | Details |
| A | TYR900 | |
| C | TYR900 |
