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1KPL

Crystal Structure of the ClC Chloride Channel from S. typhimurium

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
A0055085biological_processtransmembrane transport
A1902476biological_processchloride transmembrane transport
B0005247molecular_functionvoltage-gated chloride channel activity
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006821biological_processchloride transport
B0015108molecular_functionchloride transmembrane transporter activity
B0015297molecular_functionantiporter activity
B0016020cellular_componentmembrane
B0055085biological_processtransmembrane transport
B1902476biological_processchloride transmembrane transport
C0005247molecular_functionvoltage-gated chloride channel activity
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0006821biological_processchloride transport
C0015108molecular_functionchloride transmembrane transporter activity
C0015297molecular_functionantiporter activity
C0016020cellular_componentmembrane
C0055085biological_processtransmembrane transport
C1902476biological_processchloride transmembrane transport
D0005247molecular_functionvoltage-gated chloride channel activity
D0005886cellular_componentplasma membrane
D0006811biological_processmonoatomic ion transport
D0006821biological_processchloride transport
D0015108molecular_functionchloride transmembrane transporter activity
D0015297molecular_functionantiporter activity
D0016020cellular_componentmembrane
D0055085biological_processtransmembrane transport
D1902476biological_processchloride transmembrane transport
Functional Information from PDB Data
site_idAC1
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL A 503
ChainResidue
ASER107
AGLY355
AILE356
APHE357
ATYR445

site_idAC2
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL B 504
ChainResidue
BTYR445
BSER107
BGLY355
BILE356
BPHE357

site_idAC3
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 505
ChainResidue
AARG209
BARG17
DMET168
DARG169
DSER170

site_idAC4
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 A 506
ChainResidue
AARG205
AARG209
AASN211
ALEU212
AILE213
BARG205
BARG209

site_idAC5
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL C 603
ChainResidue
CSER107
CGLY355
CILE356
CPHE357
CTYR445

site_idAC6
Number of Residues5
DetailsBINDING SITE FOR RESIDUE CL D 604
ChainResidue
DSER107
DGLY355
DILE356
DPHE357
DTYR445

site_idAC7
Number of Residues5
DetailsBINDING SITE FOR RESIDUE SO4 B 605
ChainResidue
BMET168
BARG169
BSER170
CARG209
DARG17

site_idAC8
Number of Residues7
DetailsBINDING SITE FOR RESIDUE SO4 C 606
ChainResidue
CARG205
CARG209
CASN211
CLEU212
CILE213
DARG205
DARG209

site_idAC9
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MYS B 501
ChainResidue
AILE227
BLEU256

site_idBC1
Number of Residues2
DetailsBINDING SITE FOR RESIDUE MYS D 601
ChainResidue
CILE227
DLEU256

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues868
DetailsTransmembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues208
DetailsTopological domain: {"description":"Periplasmic"}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues208
DetailsIntramembrane: {"description":"Helical"}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues144
DetailsTopological domain: {"description":"Cytoplasmic"}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues32
DetailsIntramembrane: {"description":"Note=Loop between two helices"}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues16
DetailsMotif: {"description":"Selectivity filter part_1"}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues16
DetailsMotif: {"description":"Selectivity filter part_2"}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues16
DetailsMotif: {"description":"Selectivity filter part_3"}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues16
DetailsBinding site: {}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues4
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_FI11
Number of Residues4
DetailsSite: {"description":"Mediates proton transfer from the protein to the inner aqueous phase"}
ChainResidueDetails

245011

PDB entries from 2025-11-19

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