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7CQ6

Structure of the human CLCN7-OSTM1 complex

Functional Information from GO Data
ChainGOidnamespacecontents
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
D0000166molecular_functionnucleotide binding
D0005254molecular_functionchloride channel activity
D0005515molecular_functionprotein binding
D0005524molecular_functionATP binding
D0005764cellular_componentlysosome
D0005765cellular_componentlysosomal membrane
D0006811biological_processmonoatomic ion transport
D0006821biological_processchloride transport
D0009268biological_processresponse to pH
D0015108molecular_functionchloride transmembrane transporter activity
D0015297molecular_functionantiporter activity
D0016020cellular_componentmembrane
D0030321biological_processtransepithelial chloride transport
D0034707cellular_componentchloride channel complex
D0055085biological_processtransmembrane transport
D0062158molecular_functionchloride:proton antiporter activity
D1902476biological_processchloride transmembrane transport
D1902600biological_processproton transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues40
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues18
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues444
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues104
DetailsIntramembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues10
DetailsIntramembrane: {"description":"Note=Loop between two helices","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsMotif: {"description":"Selectivity filter part_1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsMotif: {"description":"Selectivity filter part_2","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues8
DetailsMotif: {"description":"Selectivity filter part_3","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues16
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
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_FI11
Number of Residues2
DetailsSite: {"description":"Mediates proton transfer from the protein to the inner aqueous phase","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

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PDB entries from 2025-07-30

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