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4BKJ

Crystal structure of the human DDR1 kinase domain in complex with imatinib

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
A0016020cellular_componentmembrane
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
B0016020cellular_componentmembrane
Functional Information from PDB Data
site_idAC1
Number of Residues16
DetailsBINDING SITE FOR RESIDUE STI A 1000
ChainResidue
AVAL624
AVAL763
AHIS764
ALEU773
AALA783
AASP784
APHE785
AHOH2208
AALA653
ALYS655
AGLU672
AMET676
AILE685
ATHR701
ATYR703
AMET704

site_idAC2
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO A 1001
ChainResidue
AASN706
APHE712
AGLY775
AGLU776
AASN777
APHE778
AHOH2083
AHOH2120

site_idAC3
Number of Residues10
DetailsBINDING SITE FOR RESIDUE EDO A 1002
ChainResidue
AMET810
AALA811
ATRP812
AILE815
ATRP827
APHE845
AVAL853
AASN856
AALA857
AEDO1007

site_idAC4
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1003
ChainResidue
ATRP812
AGLU813
AARG890
ASER892

site_idAC5
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1004
ChainResidue
ATHR822
APRO897
APHE898
ASER899
AEDO1006
AHOH2197

site_idAC6
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1005
ChainResidue
AASN683
AALA748
AGLN749
ASER752
AHIS902
AHOH2071

site_idAC7
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1006
ChainResidue
ATHR822
AALA823
ASER892
AARG895
APRO897
AVAL913
AEDO1004

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1007
ChainResidue
ATRP827
APHE845
ATYR869
ALEU870
ATRP888
AEDO1002
AHOH2133

site_idAC9
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1008
ChainResidue
AASP634
AVAL636
APHE712
AHIS716
APRO736
ATHR737
AHOH2026

site_idBC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1009
ChainResidue
AHIS745
AGLN749
AASN777
ATHR779
AHOH2071

site_idBC2
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO A 1010
ChainResidue
AHOH2211
BASP668
BGLU672

site_idBC3
Number of Residues17
DetailsBINDING SITE FOR RESIDUE STI B 1000
ChainResidue
BVAL624
BALA653
BLYS655
BGLU672
BMET676
BILE685
BMET699
BTHR701
BTYR703
BMET704
BVAL763
BHIS764
BLEU773
BALA783
BASP784
BPHE785
BHOH2160

site_idBC4
Number of Residues3
DetailsBINDING SITE FOR RESIDUE EDO B 1001
ChainResidue
BVAL913
BEDO1002
BHOH2158

site_idBC5
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 1002
ChainResidue
BCYS876
BPRO877
BEDO1001
BHOH2128

site_idBC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 1003
ChainResidue
BARG895
BPRO897
BVAL913
BEDO1004
BHOH2159

site_idBC7
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO B 1004
ChainResidue
BTHR822
BPRO897
BPHE898
BSER899
BEDO1003
BHOH2149

site_idBC8
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 1005
ChainResidue
BGLU813
BARG890
BGLU891
BSER892

site_idBC9
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO B 1006
ChainResidue
BASN706
BGLY775
BGLU776
BASN777
BPHE778

site_idCC1
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 1007
ChainResidue
BILE807
BARG808
BMET810
BILE815
BPHE845
BVAL853
BASN856
BHOH2086

site_idCC2
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO B 1008
ChainResidue
BGLY818
BLYS819
BPHE820
BASN911

site_idCC3
Number of Residues8
DetailsBINDING SITE FOR RESIDUE EDO B 1009
ChainResidue
AARG607
ALEU610
AILE656
AHOH2008
AHOH2021
BGLN847
BTHR849
BGLN852

Functional Information from PROSITE/UniProt
site_idPS00109
Number of Residues13
DetailsPROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLATRNCLV
ChainResidueDetails
APHE762-VAL774

site_idPS00239
Number of Residues9
DetailsRECEPTOR_TYR_KIN_II Receptor tyrosine kinase class II signature. NLYagdYYR
ChainResidueDetails
AASN790-ARG798

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: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues2
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16337946","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"24509848","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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