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6MOB

Crystal structure of KIT1 in complex with DP2976 via co-crystallization

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 Residues6
Detailsbinding site for residue NO3 A 1001
ChainResidue
AARG586
APHE591
APRO665
ALEU667
AHOH1226
AHOH1274

site_idAC2
Number of Residues4
Detailsbinding site for residue NO3 A 1002
ChainResidue
AHOH1184
AALA597
ALYS602
ALYS626

site_idAC3
Number of Residues8
Detailsbinding site for residue NO3 A 1003
ChainResidue
AGLY598
AALA599
APHE600
AGLY601
ALEU813
AARG815
AHOH1241
AHOH1250

site_idAC4
Number of Residues4
Detailsbinding site for residue NO3 A 1004
ChainResidue
AARG634
APRO665
ATHR666
AHOH1130

site_idAC5
Number of Residues5
Detailsbinding site for residue NO3 A 1005
ChainResidue
ATHR574
AGLU635
AMET638
ASER639
ALYS642

site_idAC6
Number of Residues7
Detailsbinding site for residue NO3 A 1006
ChainResidue
ALYS581
ATRP582
AGLU583
APHE584
ALEU657
AGLY658
AHOH1142

site_idAC7
Number of Residues7
Detailsbinding site for residue NO3 A 1007
ChainResidue
ALYS834
ASER868
ATYR870
APRO871
AGLY872
AMET873
AHOH1133

site_idAC8
Number of Residues7
Detailsbinding site for residue NO3 A 1008
ChainResidue
ATYR675
APHE681
AARG684
ALYS685
ALEU762
AARG804
AHOH1108

site_idAC9
Number of Residues5
Detailsbinding site for residue NO3 A 1009
ChainResidue
AARG683
AARG686
AGLY866
ASER867
AHOH1139

site_idAD1
Number of Residues6
Detailsbinding site for residue NO3 A 1010
ChainResidue
ATRP860
APRO871
AMET889
ALEU890
AHOH1118
AHOH1161

site_idAD2
Number of Residues6
Detailsbinding site for residue NO3 A 1011
ChainResidue
ATYR870
AMET873
AMET882
AILE883
APHE887
AARG888

site_idAD3
Number of Residues9
Detailsbinding site for residue NO3 A 1012
ChainResidue
AASN587
AARG588
ATYR609
APHE887
AARG888
AHOH1157
AHOH1159
AHOH1265
AHOH1304

site_idAD4
Number of Residues5
Detailsbinding site for residue NO3 A 1013
ChainResidue
ALYS613
AALA616
AALA617
AMET618
AHOH1102

site_idAD5
Number of Residues3
Detailsbinding site for residue NO3 A 1014
ChainResidue
AALA616
AALA617
AGLU885

site_idAD6
Number of Residues17
Detailsbinding site for residue JWY A 1015
ChainResidue
AVAL603
AALA621
ALYS623
AGLU640
ALEU644
AILE653
AVAL654
AVAL668
ATHR670
AGLU671
ACYS673
ALEU799
AILE808
ACYS809
AASP810
APHE811
AHOH1217

Functional Information from PROSITE/UniProt
site_idPS00107
Number of Residues29
DetailsPROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGAGAFGKVVeAtaygliksdaamt.....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. GnHmNIVNLLGACT
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":"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_FI5
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_FI6
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"7539802","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"20147452","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"12878163","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
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

245011

PDB entries from 2025-11-19

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