6JQR
Crystal structure of FLT3 in complex with gilteritinib
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 | 10 |
| Details | binding site for residue C6F A 1001 |
| Chain | Residue |
| A | LEU616 |
| A | PHE830 |
| A | ALA642 |
| A | GLU692 |
| A | TYR693 |
| A | CYS694 |
| A | CYS695 |
| A | GLY697 |
| A | ASP698 |
| A | LEU818 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | binding site for residue SO4 A 1002 |
| Chain | Residue |
| A | GLU604 |
| A | PHE605 |
| A | ARG607 |
| A | CYS681 |
| A | THR682 |
| A | LEU683 |
| A | SER684 |
| A | VAL844 |
| A | GLY846 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 A 1003 |
| Chain | Residue |
| A | GLN580 |
| A | ARG704 |
| A | ASN841 |
| A | HOH1139 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | binding site for residue SO4 A 1004 |
| Chain | Residue |
| A | TYR696 |
| A | HIS821 |
| A | GLY822 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | binding site for residue GOL A 1006 |
| Chain | Residue |
| A | LYS907 |
| A | ALA927 |
| A | PHE928 |
| A | ASP929 |
| A | LYS932 |
| site_id | AC6 |
| Number of Residues | 9 |
| Details | binding site for residue CXS A 1007 |
| Chain | Residue |
| A | GLN580 |
| A | PHE590 |
| A | VAL592 |
| A | TYR597 |
| A | ARG704 |
| A | ARG707 |
| A | GLY885 |
| A | VAL886 |
| A | ASN887 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | binding site for residue GOL A 1008 |
| Chain | Residue |
| A | PRO893 |
| A | ASN897 |
| A | HOH1102 |
| A | HOH1102 |
| A | HOH1103 |
| A | HOH1103 |
| A | HOH1106 |
| A | HOH1106 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 29 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFGKVMnAtaygisktgvsiq.....VAVK |
| Chain | Residue | Details |
| A | LEU616-LYS644 |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CVHrDLAARNVLV |
| Chain | Residue | Details |
| A | CYS807-VAL819 |
| site_id | PS00240 |
| Number of Residues | 14 |
| Details | RECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GsHeNIVNLLGACT |
| Chain | Residue | Details |
| A | GLY669-THR682 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Region: {"description":"Important for normal regulation of the kinase activity and for maintaining the kinase in an inactive state in the absence of bound ligand"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| 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_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"16684964","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21262971","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"16684964","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16684964","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19477218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21262971","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"15831474","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16627759","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16684964","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19477218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21262971","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19477218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21262971","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI10 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16627759","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19477218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21262971","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
