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6HP9

Structure of the kinase domain of human DDR1 in complex with a 2-Amino-2,3-Dihydro-1H-Indene-5-Carboxamide-based inhibitor

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 Residues17
Detailsbinding site for residue GKB A 1001
ChainResidue
AALA653
ATYR703
AMET704
APHE762
AHIS764
AALA783
AASP784
AHOH1101
AHOH1175
AGLU672
AILE675
AMET676
ALEU679
AILE684
AILE685
ATHR701
AASP702

site_idAC2
Number of Residues17
Detailsbinding site for residue GKB B 1001
ChainResidue
BALA653
BGLU672
BILE675
BMET676
BLEU679
BILE684
BILE685
BTHR701
BASP702
BTYR703
BMET704
BPHE762
BHIS764
BALA783
BASP784
BGLN847
BHOH1129

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 2024-07-17

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