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8HVT

Structure of the human CLC-7/Ostm1 complex reveals a novel state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005254molecular_functionchloride channel activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005764cellular_componentlysosome
A0005765cellular_componentlysosomal membrane
A0006811biological_processmonoatomic ion transport
A0006821biological_processchloride transport
A0009268biological_processresponse to pH
A0015108molecular_functionchloride transmembrane transporter activity
A0015297molecular_functionantiporter activity
A0016020cellular_componentmembrane
A0030321biological_processtransepithelial chloride transport
A0034707cellular_componentchloride channel complex
A0055085biological_processtransmembrane transport
A0062158molecular_functionchloride:proton antiporter activity
A1902476biological_processchloride transmembrane transport
A1902600biological_processproton transmembrane transport
C0000166molecular_functionnucleotide binding
C0005254molecular_functionchloride channel activity
C0005515molecular_functionprotein binding
C0005524molecular_functionATP binding
C0005764cellular_componentlysosome
C0005765cellular_componentlysosomal membrane
C0006811biological_processmonoatomic ion transport
C0006821biological_processchloride transport
C0009268biological_processresponse to pH
C0015108molecular_functionchloride transmembrane transporter activity
C0015297molecular_functionantiporter activity
C0016020cellular_componentmembrane
C0030321biological_processtransepithelial chloride transport
C0034707cellular_componentchloride channel complex
C0055085biological_processtransmembrane transport
C0062158molecular_functionchloride:proton antiporter activity
C1902476biological_processchloride transmembrane transport
C1902600biological_processproton transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues444
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues104
DetailsIntramembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues10
DetailsIntramembrane: {"description":"Note=Loop between two helices","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues8
DetailsMotif: {"description":"Selectivity filter part_1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsMotif: {"description":"Selectivity filter part_2","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsMotif: {"description":"Selectivity filter part_3","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues6
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues2
DetailsSite: {"description":"Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues2
DetailsSite: {"description":"Mediates proton transfer from the protein to the inner aqueous phase","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues40
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues16
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

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