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4XUF

Crystal structure of the FLT3 kinase domain bound to the inhibitor quizartinib (AC220)

Functional Information from GO Data
ChainGOidnamespacecontents
A0004672molecular_functionprotein kinase activity
A0004713molecular_functionprotein tyrosine kinase activity
A0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
A0005524molecular_functionATP binding
A0006468biological_processprotein phosphorylation
A0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
B0004672molecular_functionprotein kinase activity
B0004713molecular_functionprotein tyrosine kinase activity
B0004714molecular_functiontransmembrane receptor protein tyrosine kinase activity
B0005524molecular_functionATP binding
B0006468biological_processprotein phosphorylation
B0007169biological_processcell surface receptor protein tyrosine kinase signaling pathway
Functional Information from PDB Data
site_idAC1
Number of Residues17
Detailsbinding site for residue P30 A 1001
ChainResidue
ALEU616
ACYS695
ATYR696
AGLY697
AHIS809
ALEU818
AILE827
ACYS828
AASP829
ATYR630
AALA642
AGLU661
AMET664
AMET665
AILE674
AVAL675
ACYS694

site_idAC2
Number of Residues17
Detailsbinding site for residue P30 B 1001
ChainResidue
BASN609
BLEU616
BTYR630
BALA642
BLYS644
BGLU661
BMET664
BMET665
BILE674
BTYR693
BCYS694
BCYS695
BHIS809
BLEU818
BCYS828
BASP829
BPHE830

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGAFGKVMnAtaygisktgvsiq.....VAVK
ChainResidueDetails
ALEU616-LYS644

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CVHrDLAARNVLV
ChainResidueDetails
ACYS807-VAL819

site_idPS00240
Number of Residues14
DetailsRECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GsHeNIVNLLGACT
ChainResidueDetails
AGLY669-THR682

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsActive site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues16
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues2
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19477218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21262971","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified 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"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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