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5VRE

Crystal structure of a lysosomal potassium-selective channel TMEM175 homolog from Chamaesiphon Minutus

Functional Information from GO Data
ChainGOidnamespacecontents
A0005267molecular_functionpotassium channel activity
A0006811biological_processmonoatomic ion transport
A0006813biological_processpotassium ion transport
A0015252molecular_functionproton channel activity
A0016020cellular_componentmembrane
A0034220biological_processmonoatomic ion transmembrane transport
A0042802molecular_functionidentical protein binding
A0051289biological_processprotein homotetramerization
A0071805biological_processpotassium ion transmembrane transport
A1902600biological_processproton transmembrane transport
B0005267molecular_functionpotassium channel activity
B0006811biological_processmonoatomic ion transport
B0006813biological_processpotassium ion transport
B0015252molecular_functionproton channel activity
B0016020cellular_componentmembrane
B0034220biological_processmonoatomic ion transmembrane transport
B0042802molecular_functionidentical protein binding
B0051289biological_processprotein homotetramerization
B0071805biological_processpotassium ion transmembrane transport
B1902600biological_processproton transmembrane transport
C0005267molecular_functionpotassium channel activity
C0006811biological_processmonoatomic ion transport
C0006813biological_processpotassium ion transport
C0015252molecular_functionproton channel activity
C0016020cellular_componentmembrane
C0034220biological_processmonoatomic ion transmembrane transport
C0042802molecular_functionidentical protein binding
C0051289biological_processprotein homotetramerization
C0071805biological_processpotassium ion transmembrane transport
C1902600biological_processproton transmembrane transport
D0005267molecular_functionpotassium channel activity
D0006811biological_processmonoatomic ion transport
D0006813biological_processpotassium ion transport
D0015252molecular_functionproton channel activity
D0016020cellular_componentmembrane
D0034220biological_processmonoatomic ion transmembrane transport
D0042802molecular_functionidentical protein binding
D0051289biological_processprotein homotetramerization
D0071805biological_processpotassium ion transmembrane transport
D1902600biological_processproton transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues92
DetailsTransmembrane: {"description":"Helical; Name=TM1","evidences":[{"source":"PubMed","id":"28723891","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues108
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"PubMed","id":"28723891","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues100
DetailsTransmembrane: {"description":"Helical; Name=TM2","evidences":[{"source":"PubMed","id":"28723891","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues32
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"PubMed","id":"28723891","evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues100
DetailsTransmembrane: {"description":"Helical; Name=TM3","evidences":[{"source":"PubMed","id":"28723891","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues96
DetailsTransmembrane: {"description":"Helical; Name=TM4","evidences":[{"source":"PubMed","id":"28723891","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues104
DetailsTransmembrane: {"description":"Helical; Name=TM5","evidences":[{"source":"PubMed","id":"28723891","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues60
DetailsTransmembrane: {"description":"Helical; Name=TM6","evidences":[{"source":"PubMed","id":"28723891","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues20
DetailsRegion: {"description":"Short helix H1","evidences":[{"source":"PubMed","id":"28723891","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues24
DetailsRegion: {"description":"Short helix H2","evidences":[{"source":"PubMed","id":"28723891","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues24
DetailsMotif: {"description":"RxxxFSD motif","evidences":[{"source":"PubMed","id":"28723891","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues4
DetailsSite: {"description":"Hydrophobic filter residue 1","evidences":[{"source":"PubMed","id":"28723891","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues4
DetailsSite: {"description":"Hydrophobic filter residue 2","evidences":[{"source":"PubMed","id":"28723891","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues4
DetailsSite: {"description":"Hydrophobic filter residue 3","evidences":[{"source":"PubMed","id":"28723891","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

243531

PDB entries from 2025-10-22

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