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6CUD

Structure of the human TRPC3 in a lipid-occupied, closed state

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005262molecular_functioncalcium channel activity
A0006811biological_processmonoatomic ion transport
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
A0070588biological_processcalcium ion transmembrane transport
B0005216molecular_functionmonoatomic ion channel activity
B0005262molecular_functioncalcium channel activity
B0006811biological_processmonoatomic ion transport
B0016020cellular_componentmembrane
B0055085biological_processtransmembrane transport
B0070588biological_processcalcium ion transmembrane transport
C0005216molecular_functionmonoatomic ion channel activity
C0005262molecular_functioncalcium channel activity
C0006811biological_processmonoatomic ion transport
C0016020cellular_componentmembrane
C0055085biological_processtransmembrane transport
C0070588biological_processcalcium ion transmembrane transport
D0005216molecular_functionmonoatomic ion channel activity
D0005262molecular_functioncalcium channel activity
D0006811biological_processmonoatomic ion transport
D0016020cellular_componentmembrane
D0055085biological_processtransmembrane transport
D0070588biological_processcalcium ion transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues508
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:29726814
ChainResidueDetails
AVAL375-ALA392
BPRO522-LEU545
BILE565-SER588
BLYS629-LEU654
CVAL375-ALA392
CTRP424-LYS442
CLEU456-LEU477
CPRO522-LEU545
CILE565-SER588
CLYS629-LEU654
DVAL375-ALA392
ATRP424-LYS442
DTRP424-LYS442
DLEU456-LEU477
DPRO522-LEU545
DILE565-SER588
DLYS629-LEU654
ALEU456-LEU477
APRO522-LEU545
AILE565-SER588
ALYS629-LEU654
BVAL375-ALA392
BTRP424-LYS442
BLEU456-LEU477

site_idSWS_FT_FI2
Number of Residues448
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:29726814
ChainResidueDetails
ASER393-THR423
DSER393-THR423
DALA478-ASP521
DTYR589-HIS628
AALA478-ASP521
ATYR589-HIS628
BSER393-THR423
BALA478-ASP521
BTYR589-HIS628
CSER393-THR423
CALA478-ASP521
CTYR589-HIS628

site_idSWS_FT_FI3
Number of Residues120
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:29726814
ChainResidueDetails
AGLU443-GLN455
APRO546-ASP564
BGLU443-GLN455
BPRO546-ASP564
CGLU443-GLN455
CPRO546-ASP564
DGLU443-GLN455
DPRO546-ASP564

site_idSWS_FT_FI4
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:35051376, ECO:0007744|PDB:7DXB, ECO:0007744|PDB:7DXD
ChainResidueDetails
AGLU73
AASP798
BGLU73
BASP798
CGLU73
CASP798
DGLU73
DASP798

site_idSWS_FT_FI5
Number of Residues24
DetailsBINDING: BINDING => ECO:0000269|PubMed:35051376, ECO:0007744|PDB:7DXB
ChainResidueDetails
AGLU440
BGLU786
BGLU789
BGLU791
CGLU440
CGLU443
CASN458
CGLU786
CGLU789
CGLU791
DGLU440
AGLU443
DGLU443
DASN458
DGLU786
DGLU789
DGLU791
AASN458
AGLU786
AGLU789
AGLU791
BGLU440
BGLU443
BASN458

site_idSWS_FT_FI6
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:29726814, ECO:0000269|PubMed:9535843, ECO:0007744|PDB:6CUD
ChainResidueDetails
AASN404
BASN404
CASN404
DASN404

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PDB entries from 2024-07-31

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