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8JPR

Cryo-EM structure of Y553C human ClC-6

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0005247molecular_functionvoltage-gated chloride channel activity
A0005254molecular_functionchloride channel activity
A0005524molecular_functionATP binding
A0005765cellular_componentlysosomal membrane
A0006811biological_processmonoatomic ion transport
A0006821biological_processchloride transport
A0006884biological_processcell volume homeostasis
A0007165biological_processsignal transduction
A0009612biological_processresponse to mechanical stimulus
A0010008cellular_componentendosome membrane
A0015108molecular_functionchloride transmembrane transporter activity
A0015297molecular_functionantiporter activity
A0016020cellular_componentmembrane
A0031902cellular_componentlate endosome membrane
A0034220biological_processmonoatomic ion transmembrane transport
A0055085biological_processtransmembrane transport
A1902476biological_processchloride transmembrane transport
B0000166molecular_functionnucleotide binding
B0005247molecular_functionvoltage-gated chloride channel activity
B0005254molecular_functionchloride channel activity
B0005524molecular_functionATP binding
B0005765cellular_componentlysosomal membrane
B0006811biological_processmonoatomic ion transport
B0006821biological_processchloride transport
B0006884biological_processcell volume homeostasis
B0007165biological_processsignal transduction
B0009612biological_processresponse to mechanical stimulus
B0010008cellular_componentendosome membrane
B0015108molecular_functionchloride transmembrane transporter activity
B0015297molecular_functionantiporter activity
B0016020cellular_componentmembrane
B0031902cellular_componentlate endosome membrane
B0034220biological_processmonoatomic ion transmembrane transport
B0055085biological_processtransmembrane transport
B1902476biological_processchloride transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues434
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 Residues122
DetailsDomain: {"description":"CBS 2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00703","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues8
DetailsMotif: {"description":"Selectivity filter part_1","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsMotif: {"description":"Selectivity filter part_2","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues8
DetailsMotif: {"description":"Selectivity filter part_3","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues16
DetailsBinding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
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_FI10
Number of Residues2
DetailsSite: {"description":"Mediates proton transfer from the protein to the inner aqueous phase","evidences":[{"evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues2
DetailsModified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"O35454","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"17534424","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

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PDB entries from 2025-10-08

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