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4HVS

Crystal structure of KIT kinase domain with a small molecule inhibitor, PLX647

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
Functional Information from PDB Data
site_idAC1
Number of Residues17
DetailsBINDING SITE FOR RESIDUE 647 A 1001
ChainResidue
ATRP557
ATYR672
ACYS673
ALEU783
AHIS790
ALEU799
AILE808
ACYS809
AASP810
AALA621
ALYS623
AGLU640
ALEU647
AILE653
AVAL654
ATHR670
AGLU671

Functional Information from PROSITE/UniProt
site_idPS00024
Number of Residues16
DetailsHEMOPEXIN Hemopexin domain signature. LPvkWmapEsIFNSVY
ChainResidueDetails
ALEU831-TYR846

site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGAFGKVVeAtaqgliksdaamt.....VAVK
ChainResidueDetails
ALEU595-LYS623

site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. CIHrDLAARNILL
ChainResidueDetails
ACYS788-LEU800

site_idPS00240
Number of Residues14
DetailsRECEPTOR_TYR_KIN_III Receptor tyrosine kinase class III signature. GnHeNIVNLLGACT
ChainResidueDetails
AGLY648-THR661

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsRegion: {"description":"Important for interaction with phosphotyrosine-binding proteins"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
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_FI3
Number of Residues18
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"20147452","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified 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"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"12824176","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9038210","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"7539802","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"20147452","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"12878163","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"12878163","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"20147452","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

240971

PDB entries from 2025-08-27

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