4XUF
Crystal structure of the FLT3 kinase domain bound to the inhibitor quizartinib (AC220)
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 | 17 |
Details | binding site for residue P30 A 1001 |
Chain | Residue |
A | LEU616 |
A | CYS695 |
A | TYR696 |
A | GLY697 |
A | HIS809 |
A | LEU818 |
A | ILE827 |
A | CYS828 |
A | ASP829 |
A | TYR630 |
A | ALA642 |
A | GLU661 |
A | MET664 |
A | MET665 |
A | ILE674 |
A | VAL675 |
A | CYS694 |
site_id | AC2 |
Number of Residues | 17 |
Details | binding site for residue P30 B 1001 |
Chain | Residue |
B | ASN609 |
B | LEU616 |
B | TYR630 |
B | ALA642 |
B | LYS644 |
B | GLU661 |
B | MET664 |
B | MET665 |
B | ILE674 |
B | TYR693 |
B | CYS694 |
B | CYS695 |
B | HIS809 |
B | LEU818 |
B | CYS828 |
B | ASP829 |
B | PHE830 |
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 | 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_FI2 |
Number of Residues | 16 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]} |
Chain | Residue | Details |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
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_FI5 |
Number of Residues | 2 |
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 |