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5BVO

Fragment-based discovery of potent and selective DDR1/2 inhibitors

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 Residues1
Detailsbinding site for residue IOD A 1002
ChainResidue
AGLN900

site_idAC2
Number of Residues2
Detailsbinding site for residue IOD A 1003
ChainResidue
AGLY622
AVAL624

site_idAC3
Number of Residues4
Detailsbinding site for residue IOD A 1004
ChainResidue
AASP681
APRO682
AARG686
AHOH1307

site_idAC4
Number of Residues1
Detailsbinding site for residue IOD A 1005
ChainResidue
AHIS902

site_idAC5
Number of Residues2
Detailsbinding site for residue IOD A 1006
ChainResidue
ASER739
APRO659

site_idAC6
Number of Residues2
Detailsbinding site for residue IOD A 1007
ChainResidue
AGLY617
AGLU618

site_idAC7
Number of Residues14
Detailsbinding site for residue 4VE A 1008
ChainResidue
AALA653
ALYS655
AGLU672
AMET676
ALEU679
AILE685
ATHR701
AASP702
AMET704
APHE762
ALEU773
AALA783
AASP784
APHE785

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
DetailsACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10028
ChainResidueDetails
APHE785

site_idSWS_FT_FI2
Number of Residues1
DetailsBINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159
ChainResidueDetails
ALEU635

site_idSWS_FT_FI3
Number of Residues1
DetailsBINDING:
ChainResidueDetails
ALYS674

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19369195
ChainResidueDetails
ALEU650

site_idSWS_FT_FI5
Number of Residues1
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000305|PubMed:16337946
ChainResidueDetails
ATHR759

site_idSWS_FT_FI6
Number of Residues3
DetailsMOD_RES: Phosphotyrosine; by autocatalysis => ECO:0000269|PubMed:24509848
ChainResidueDetails
AALA811
AILE815
ALEU816

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PDB entries from 2024-07-17

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