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5FDP

Structure of DDR1 receptor tyrosine kinase in complex with D2099 inhibitor at 2.25 Angstroms resolution.

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 Residues16
Detailsbinding site for residue 5WR A 1001
ChainResidue
AALA653
ATYR703
AMET704
APHE762
AHIS764
AALA783
AASP784
AHOH1190
ALYS655
AGLU672
AMET676
ALEU679
AILE685
AMET699
ATHR701
AASP702

site_idAC2
Number of Residues8
Detailsbinding site for residue PEG A 1002
ChainResidue
AASN710
AALA768
ATHR769
AARG770
AASP795
ATRP809
AGLU835
AALA842

site_idAC3
Number of Residues3
Detailsbinding site for residue EDO A 1003
ChainResidue
AMET817
AGLY818
AARG841

site_idAC4
Number of Residues4
Detailsbinding site for residue EDO A 1004
ChainResidue
AHIS745
AALA748
AHIS902
AHOH1110

site_idAC5
Number of Residues2
Detailsbinding site for residue EDO A 1005
ChainResidue
AARG890
ASER892

site_idAC6
Number of Residues5
Detailsbinding site for residue EDO A 1006
ChainResidue
ATRP827
APHE845
ATYR869
ALEU870
ATRP888

site_idAC7
Number of Residues4
Detailsbinding site for residue EDO A 1007
ChainResidue
AALA758
ATHR759
APRO897
APHE898

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

243531

PDB entries from 2025-10-22

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