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6LSC

Structure of the E202Y mutant of the Cl-/H+ antiporter CLC-ec1 from E.coli: a re-refined model of the 4FTP model

Replaces:  4FTP
Functional Information from GO Data
ChainGOidnamespacecontents
A0005247molecular_functionvoltage-gated chloride channel activity
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006821biological_processchloride transport
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 Residues5
Detailsbinding site for residue CL A 501
ChainResidue
ASER107
AGLY355
AILE356
APHE357
ATYR445

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues63
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
AMET1-PRO32
AGLU117-ARG123
AARG167-THR176
ATYR202-SER214
AARG282-ASN287

site_idSWS_FT_FI2
Number of Residues216
DetailsTRANSMEM: Helical
ChainResidueDetails
ALEU33-VAL69
AILE422-PHE438
ALEU77-TYR100
ATRP124-GLY141
AGLU148-PHE166
AILE215-PHE232
ATRP253-HIS281
AILE288-ALA309
AMET330-SER349
AGLY355-VAL376

site_idSWS_FT_FI3
Number of Residues53
DetailsTOPO_DOM: Periplasmic
ChainResidueDetails
AHIS70-PRO76
AASN233-LEU252
APRO310-SER329
AGLU377-ALA386

site_idSWS_FT_FI4
Number of Residues52
DetailsINTRAMEM: Helical
ChainResidueDetails
AILE109-LEU116
ALEU177-ALA189
APRO193-ILE201
AGLY387-SER401
APRO405-THR416

site_idSWS_FT_FI5
Number of Residues6
DetailsINTRAMEM: Note=Loop between two helices
ChainResidueDetails
AILE402-ALA404
AASP417-LEU421

site_idSWS_FT_FI6
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12649487, ECO:0000305|PubMed:16341087, ECO:0000305|PubMed:18678918, ECO:0007744|PDB:1OTT, ECO:0007744|PDB:1OTU
ChainResidueDetails
ASER107

site_idSWS_FT_FI7
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12649487, ECO:0007744|PDB:1OTS, ECO:0007744|PDB:4ENE, ECO:0007744|PDB:6LSC
ChainResidueDetails
AILE356

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12649487, ECO:0007744|PDB:1OTT
ChainResidueDetails
APHE357

site_idSWS_FT_FI9
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:12649487, ECO:0007744|PDB:1OTS, ECO:0007744|PDB:1OTT, ECO:0007744|PDB:1OTU, ECO:0007744|PDB:4ENE, ECO:0007744|PDB:6LSC
ChainResidueDetails
ATYR445

site_idSWS_FT_FI10
Number of Residues1
DetailsSITE: Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport
ChainResidueDetails
AGLU148

site_idSWS_FT_FI11
Number of Residues1
DetailsSITE: Mediates proton transfer from the protein to the inner aqueous phase
ChainResidueDetails
AGLU203

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PDB entries from 2024-11-06

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