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6BOB

Cryo-EM structure of rat TRPV6* in nanodiscs

Functional Information from GO Data
ChainGOidnamespacecontents
A0005216molecular_functionmonoatomic ion channel activity
A0005262molecular_functioncalcium channel activity
A0006811biological_processmonoatomic ion transport
A0006816biological_processcalcium ion transport
A0016020cellular_componentmembrane
A0055085biological_processtransmembrane transport
B0005216molecular_functionmonoatomic ion channel activity
B0005262molecular_functioncalcium channel activity
B0006811biological_processmonoatomic ion transport
B0006816biological_processcalcium ion transport
B0016020cellular_componentmembrane
B0055085biological_processtransmembrane transport
C0005216molecular_functionmonoatomic ion channel activity
C0005262molecular_functioncalcium channel activity
C0006811biological_processmonoatomic ion transport
C0006816biological_processcalcium ion transport
C0016020cellular_componentmembrane
C0055085biological_processtransmembrane transport
D0005216molecular_functionmonoatomic ion channel activity
D0005262molecular_functioncalcium channel activity
D0006811biological_processmonoatomic ion transport
D0006816biological_processcalcium ion transport
D0016020cellular_componentmembrane
D0055085biological_processtransmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues488
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:27296226, ECO:0000269|PubMed:28878326
ChainResidueDetails
ATYR327-VAL347
ALEU385-PHE407
APRO423-ARG442
AGLU449-ALA468
ALEU489-PHE511
AILE556-MET576
BTYR327-VAL347
BLEU385-PHE407
BPRO423-ARG442
BGLU449-ALA468
BLEU489-PHE511
BILE556-MET576
CTYR327-VAL347
CLEU385-PHE407
CPRO423-ARG442
CGLU449-ALA468
CLEU489-PHE511
CILE556-MET576
DTYR327-VAL347
DLEU385-PHE407
DPRO423-ARG442
DGLU449-ALA468
DLEU489-PHE511
DILE556-MET576

site_idSWS_FT_FI2
Number of Residues252
DetailsTOPO_DOM: Extracellular => ECO:0000269|PubMed:27296226, ECO:0000269|PubMed:28878326
ChainResidueDetails
ATYR348-ARG384
ALEU443-GLY448
AGLN512-ASP524
AASN545-SER555
BTYR348-ARG384
BLEU443-GLY448
BGLN512-ASP524
BASN545-SER555
CTYR348-ARG384
CLEU443-GLY448
CGLN512-ASP524
CASN545-SER555
DTYR348-ARG384
DLEU443-GLY448
DGLN512-ASP524
DASN545-SER555

site_idSWS_FT_FI3
Number of Residues132
DetailsTOPO_DOM: Cytoplasmic => ECO:0000269|PubMed:27296226, ECO:0000269|PubMed:28878326
ChainResidueDetails
AARG408-GLY422
AARG469-ASP488
BARG408-GLY422
BARG469-ASP488
CARG408-GLY422
CARG469-ASP488
DARG408-GLY422
DARG469-ASP488

site_idSWS_FT_FI4
Number of Residues76
DetailsINTRAMEM: Pore-forming => ECO:0000269|PubMed:27296226, ECO:0000269|PubMed:28878326
ChainResidueDetails
ATYR525-ALA544
BTYR525-ALA544
CTYR525-ALA544
DTYR525-ALA544

site_idSWS_FT_FI5
Number of Residues4
DetailsBINDING: BINDING => ECO:0000269|PubMed:27296226, ECO:0007744|PDB:5IWK, ECO:0007744|PDB:5IWP
ChainResidueDetails
AASP541
BASP541
CASP541
DASP541

site_idSWS_FT_FI6
Number of Residues8
DetailsMOD_RES: Phosphotyrosine; by SRC => ECO:0000269|PubMed:17197020
ChainResidueDetails
ATYR161
ATYR162
BTYR161
BTYR162
CTYR161
CTYR162
DTYR161
DTYR162

site_idSWS_FT_FI7
Number of Residues4
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN357
BASN357
CASN357
DASN357

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PDB entries from 2024-05-01

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