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6V2J

Crystal structure of ClC-ec1 triple mutant (E113Q, E148Q, E203Q)

Functional Information from GO Data
ChainGOidnamespacecontents
A0005247molecular_functionvoltage-gated chloride channel activity
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006821biological_processchloride transport
A0015108molecular_functionchloride transmembrane transporter activity
A0015297molecular_functionantiporter activity
A0016020cellular_componentmembrane
A0042802molecular_functionidentical protein binding
A0055085biological_processtransmembrane transport
A0062158molecular_functionchloride:proton antiporter activity
A1902476biological_processchloride transmembrane transport
A1902600biological_processproton transmembrane transport
A1990451biological_processcellular stress response to acidic pH
Functional Information from PDB Data
site_idAC1
Number of Residues4
Detailsbinding site for residue CL A 501
ChainResidue
ASER107
AGLY355
AILE356
ATYR445

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 502
ChainResidue
ASER107
APRO110

site_idAC3
Number of Residues5
Detailsbinding site for residue CL A 503
ChainResidue
AGLY355
APHE357
AGLY146
AARG147
AGLN148

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues216
DetailsTransmembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues53
DetailsTopological domain: {"description":"Periplasmic"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues52
DetailsIntramembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues32
DetailsTopological domain: {"description":"Cytoplasmic"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsIntramembrane: {"description":"Note=Loop between two helices"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsMotif: {"description":"Selectivity filter part_1"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsMotif: {"description":"Selectivity filter part_2"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues4
DetailsMotif: {"description":"Selectivity filter part_3"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12649487","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16341087","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"18678918","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"1OTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OTU","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12649487","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OTS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ENE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6LSC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12649487","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OTT","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"12649487","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1OTS","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OTT","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"1OTU","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"4ENE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"6LSC","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI13
Number of Residues1
DetailsSite: {"description":"Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport"}
ChainResidueDetails

site_idSWS_FT_FI14
Number of Residues1
DetailsSite: {"description":"Mediates proton transfer from the protein to the inner aqueous phase"}
ChainResidueDetails

245663

PDB entries from 2025-12-03

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