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5FDX

Structure of DDR1 receptor tyrosine kinase in complex with D2164 inhibitor at 2.65 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
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 Residues14
Detailsbinding site for residue 5X1 A 1001
ChainResidue
AALA653
AMET704
APHE762
AHIS764
AALA783
AASP784
ALYS655
AGLU672
AMET676
ALEU679
AILE684
AILE685
ATHR701
AASP702

site_idAC2
Number of Residues6
Detailsbinding site for residue EDO A 1002
ChainResidue
ATRP812
AILE815
AVAL853
AASN856
AALA857
AEDO1004

site_idAC3
Number of Residues4
Detailsbinding site for residue EDO A 1003
ChainResidue
ASER714
ACYS840
AARG841
BMET817

site_idAC4
Number of Residues5
Detailsbinding site for residue EDO A 1004
ChainResidue
ATRP827
ATYR869
ALEU870
ATRP888
AEDO1002

site_idAC5
Number of Residues1
Detailsbinding site for residue EDO A 1005
ChainResidue
AHIS648

site_idAC6
Number of Residues1
Detailsbinding site for residue PEG A 1006
ChainResidue
BGLN900

site_idAC7
Number of Residues15
Detailsbinding site for residue 5X1 B 1001
ChainResidue
BALA653
BGLU672
BMET676
BLEU679
BILE684
BILE685
BMET699
BTHR701
BASP702
BTYR703
BMET704
BPHE762
BHIS764
BALA783
BASP784

site_idAC8
Number of Residues1
Detailsbinding site for residue EDO B 1002
ChainResidue
BPHE861

site_idAC9
Number of Residues5
Detailsbinding site for residue PEG B 1003
ChainResidue
BILE815
BTRP827
BPHE845
BLEU870
BTRP888

site_idAD1
Number of Residues2
Detailsbinding site for residue PEG B 1004
ChainResidue
BALA803
BVAL804

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
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
AASP766
BASP766

site_idSWS_FT_FI2
Number of Residues2
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU616
BLEU616

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING:
ChainResidueDetails
ALYS655
BLYS655

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ASER631
BSER631

site_idSWS_FT_FI5
Number of Residues2
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:16337946
ChainResidueDetails
ATYR740
BTYR740

site_idSWS_FT_FI6
Number of Residues6
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:24509848
ChainResidueDetails
ATYR792
ATYR796
ATYR797
BTYR792
BTYR796
BTYR797

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PDB entries from 2024-07-10

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