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5HD8

Crystal structure of disulfide cross-linked D417C ClC-ec1

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
B0005247molecular_functionvoltage-gated chloride channel activity
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006821biological_processchloride transport
B0015297molecular_functionantiporter activity
B0016020cellular_componentmembrane
B0042802molecular_functionidentical protein binding
B0055085biological_processtransmembrane transport
B0062158molecular_functionchloride:proton antiporter activity
B1902476biological_processchloride transmembrane transport
B1902600biological_processproton transmembrane transport
B1990451biological_processcellular stress response to acidic pH
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue CL A 501
ChainResidue
ASER107
AILE109
AGLY355
AILE356
APHE357
ATYR445

site_idAC2
Number of Residues2
Detailsbinding site for residue CL A 502
ChainResidue
ASER107
AGLY108

site_idAC3
Number of Residues6
Detailsbinding site for residue CL B 501
ChainResidue
BILE109
BGLY355
BILE356
BPHE357
BTYR445
BSER107

site_idAC4
Number of Residues2
Detailsbinding site for residue CL B 502
ChainResidue
BSER107
BILE448

Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YTCEATH
ChainResidueDetails
DTYR191-HIS197

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues432
DetailsTRANSMEM: Helical
ChainResidueDetails
ALEU33-VAL69
AILE422-PHE438
BLEU33-VAL69
BLEU77-TYR100
BTRP124-GLY141
BGLU148-PHE166
BILE215-PHE232
BTRP253-HIS281
BILE288-ALA309
BMET330-SER349
BGLY355-VAL376
ALEU77-TYR100
BILE422-PHE438
ATRP124-GLY141
AGLU148-PHE166
AILE215-PHE232
ATRP253-HIS281
AILE288-ALA309
AMET330-SER349
AGLY355-VAL376

site_idSWS_FT_FI2
Number of Residues106
DetailsTOPO_DOM: Periplasmic
ChainResidueDetails
AHIS70-PRO76
AASN233-LEU252
APRO310-SER329
AGLU377-ALA386
BHIS70-PRO76
BASN233-LEU252
BPRO310-SER329
BGLU377-ALA386

site_idSWS_FT_FI3
Number of Residues104
DetailsINTRAMEM: Helical
ChainResidueDetails
AILE109-LEU116
BPRO405-THR416
ALEU177-ALA189
APRO193-ILE201
AGLY387-SER401
APRO405-THR416
BILE109-LEU116
BLEU177-ALA189
BPRO193-ILE201
BGLY387-SER401

site_idSWS_FT_FI4
Number of Residues64
DetailsTOPO_DOM: Cytoplasmic
ChainResidueDetails
AGLU117-ARG123
AARG167-THR176
AGLU202-SER214
AARG282-ASN287
BGLU117-ARG123
BARG167-THR176
BGLU202-SER214
BARG282-ASN287

site_idSWS_FT_FI5
Number of Residues12
DetailsINTRAMEM: Note=Loop between two helices
ChainResidueDetails
AILE402-ALA404
ACYS417-LEU421
BILE402-ALA404
BCYS417-LEU421

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12649487, ECO:0000305|PubMed:16341087, ECO:0000305|PubMed:18678918, ECO:0007744|PDB:1OTT, ECO:0007744|PDB:1OTU
ChainResidueDetails
ASER107
BSER107

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12649487, ECO:0007744|PDB:1OTS, ECO:0007744|PDB:4ENE, ECO:0007744|PDB:6LSC
ChainResidueDetails
AILE356
BILE356

site_idSWS_FT_FI8
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:12649487, ECO:0007744|PDB:1OTT
ChainResidueDetails
APHE357
BPHE357

site_idSWS_FT_FI9
Number of Residues2
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
BTYR445

site_idSWS_FT_FI10
Number of Residues2
DetailsSITE: Mediates proton transfer from the outer aqueous phase to the interior of the protein; involved in linking H(+) and Cl(-) transport
ChainResidueDetails
AGLU148
BGLU148

site_idSWS_FT_FI11
Number of Residues2
DetailsSITE: Mediates proton transfer from the protein to the inner aqueous phase
ChainResidueDetails
AGLU203
BGLU203

226707

PDB entries from 2024-10-30

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