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4CKR

Crystal structure of the human DDR1 kinase domain in complex with DDR1-IN-1

Replaces:  4BKI
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
Functional Information from PDB Data
site_idAC1
Number of Residues20
DetailsBINDING SITE FOR RESIDUE DI1 A 1000
ChainResidue
AVAL624
ATYR703
AMET704
ALEU757
AVAL763
AHIS764
AARG765
ALEU773
AILE782
AALA783
AASP784
AALA653
APHE785
ALYS655
AGLU672
AMET676
ALEU679
AILE685
ATHR701
AASP702

site_idAC2
Number of Residues7
DetailsBINDING SITE FOR RESIDUE EDO A 1001
ChainResidue
AASN706
APHE712
AVAL774
AGLY775
AGLU776
AASN777
APHE778

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1002
ChainResidue
ATHR822
APRO897
APHE898
ASER899
AEDO1004

site_idAC4
Number of Residues6
DetailsBINDING SITE FOR RESIDUE EDO A 1003
ChainResidue
AASN710
AGLU835
ACYS840
AALA842
AHOH2006
AHOH2038

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE EDO A 1004
ChainResidue
ATHR822
ASER892
AARG895
AVAL913
AEDO1002

site_idAC6
Number of Residues4
DetailsBINDING SITE FOR RESIDUE EDO A 1005
ChainResidue
AASN683
AALA748
ASER752
AHIS902

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 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_FI2
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"19369195","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues1
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16337946","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues3
DetailsModified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"24509848","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

246031

PDB entries from 2025-12-10

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