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6COZ

Human CLC-1 chloride ion channel, C-terminal cytosolic domain

Functional Information from GO Data
ChainGOidnamespacecontents
A0005247molecular_functionvoltage-gated chloride channel activity
A0005254molecular_functionchloride channel activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006821biological_processchloride transport
A0006936biological_processmuscle contraction
A0016020cellular_componentmembrane
A0019227biological_processneuronal action potential propagation
A0034220biological_processmonoatomic ion transmembrane transport
A0034702cellular_componentmonoatomic ion channel complex
A0034707cellular_componentchloride channel complex
A0042383cellular_componentsarcolemma
A0042803molecular_functionprotein homodimerization activity
A0055085biological_processtransmembrane transport
A1902476biological_processchloride transmembrane transport
B0005247molecular_functionvoltage-gated chloride channel activity
B0005254molecular_functionchloride channel activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006821biological_processchloride transport
B0006936biological_processmuscle contraction
B0016020cellular_componentmembrane
B0019227biological_processneuronal action potential propagation
B0034220biological_processmonoatomic ion transmembrane transport
B0034702cellular_componentmonoatomic ion channel complex
B0034707cellular_componentchloride channel complex
B0042383cellular_componentsarcolemma
B0042803molecular_functionprotein homodimerization activity
B0055085biological_processtransmembrane transport
B1902476biological_processchloride transmembrane transport
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1170
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
AMET1-GLY118
BTHR196-THR208
BSER247-THR268
BGLU291-ASN301
BARG377-ARG390
BASP579-LEU988
AHIS180-SER183
ATHR196-THR208
ASER247-THR268
AGLU291-ASN301
AARG377-ARG390
AASP579-LEU988
BMET1-GLY118
BHIS180-SER183

site_idSWS_FT_FI2
Number of Residues420
DetailsTRANSMEM: Helical => ECO:0000269|PubMed:29809153
ChainResidueDetails
AILE119-TYR150
APRO558-TYR578
BILE119-TYR150
BLEU159-CYS179
BMET209-PRO228
BVAL229-LEU246
BTYR302-VAL321
BLEU348-VAL376
BLEU391-PRO408
BILE458-PRO478
BILE479-VAL498
ALEU159-CYS179
BPRO558-TYR578
AMET209-PRO228
AVAL229-LEU246
ATYR302-VAL321
ALEU348-VAL376
ALEU391-PRO408
AILE458-PRO478
AILE479-VAL498

site_idSWS_FT_FI3
Number of Residues182
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
AALA151-PRO158
BLEU427-VAL457
BGLY499-PRO521
BHIS555-LEU557
ATRP322-GLU347
AGLY409-MET414
ALEU427-VAL457
AGLY499-PRO521
AHIS555-LEU557
BALA151-PRO158
BTRP322-GLU347
BGLY409-MET414

site_idSWS_FT_FI4
Number of Residues150
DetailsINTRAMEM: Helical => ECO:0000269|PubMed:29809153
ChainResidueDetails
APRO184-LYS195
AVAL269-ILE290
AALA415-THR426
AGLY522-ALA554
BPRO184-LYS195
BVAL269-ILE290
BALA415-THR426
BGLY522-ALA554

site_idSWS_FT_FI5
Number of Residues6
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P37019
ChainResidueDetails
ASER189
APHE484
ATYR578
BSER189
BPHE484
BTYR578

site_idSWS_FT_FI6
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q64347
ChainResidueDetails
ASER886
BSER886

218853

PDB entries from 2024-04-24

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