eF-site ID 6coy-AB PDB Code 6coy Chain A, B click to enlarge Title Human CLC-1 chloride ion channel, transmembrane domain Classification TRANSPORT PROTEIN Compound Chloride channel protein 1 Source (CLCN1_HUMAN) Sequence A:  EDGIFLVLLGLLMALVSWSMDYVSAKSLQAYKWSYAQMQP SLPLQFLVWVTFPLVLILFSALFCHLISPQAVGSGIPEMK TILRGVVLKEYLTMKAFVAKVVALTAGLGSGIPVGKEGPF VHIASICAAVLSKFMYYSDILTVGCAVGVGCCFGTPLGGV LFSIEVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNKDA VTITALFRTNFRMDFPFDLKELPAFAAIGICCGLLGAVFV YLHRQVMLGVRKHKALSQFLAKHRLLYPGIVTFVIASFTF PPGMGQFMAGELMPREAISTLFDNNTWVKHAGDPESLGQS AVWIHPRVNVVIIIFLFFVMKFWMSIVATTMPIPCGGFMP VFVLGAAFGRLVGEIMAMLFPDGILFDDIIYKILPGGYAV IGAAALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILA NMVAQSLQPSLYDSIIQVKKLPYLP B:  EDGIFLVLLGLLMALVSWSMDYVSAKSLQAYKWSYAQMQP SLPLQFLVWVTFPLVLILFSALFCHLISPQAVGSGIPEMK TILRGVVLKEYLTMKAFVAKVVALTAGLGSGIPVGKEGPF VHIASICAAVLSKFMYYSDILTVGCAVGVGCCFGTPLGGV LFSIEVTSTYFAVRNYWRGFFAATFSAFVFRVLAVWNKDA VTITALFRTNFRMDFPFDLKELPAFAAIGICCGLLGAVFV YLHRQVMLGVRKHKALSQFLAKHRLLYPGIVTFVIASFTF PPGMGQFMAGELMPREAISTLFDNNTWVKHAGDPESLGQS AVWIHPRVNVVIIIFLFFVMKFWMSIVATTMPIPCGGFMP VFVLGAAFGRLVGEIMAMLFPDGILFDDIIYKILPGGYAV IGAAALTGAVSHTVSTAVICFELTGQIAHILPMMVAVILA NMVAQSLQPSLYDSIIQVKKLPYLP Description Functional site 1) chain A residue 230 type sequence G description binding site for residue CL A 1001 source : AC1 2) chain A residue 231 type sequence K description binding site for residue CL A 1001 source : AC1 3) chain A residue 232 type sequence E description binding site for residue CL A 1001 source : AC1 4) chain A residue 233 type sequence G description binding site for residue CL A 1001 source : AC1 5) chain A residue 484 type sequence F description binding site for residue CL A 1001 source : AC1 6) chain A residue 485 type sequence M description binding site for residue CL A 1001 source : AC1 7) chain A residue 189 type sequence S description binding site for residue CL A 1002 source : AC2 8) chain A residue 581 type sequence I description binding site for residue CL A 1002 source : AC2 9) chain B residue 230 type sequence G description binding site for residue CL B 1001 source : AC3 10) chain B residue 231 type sequence K description binding site for residue CL B 1001 source : AC3 11) chain B residue 232 type sequence E description binding site for residue CL B 1001 source : AC3 12) chain B residue 233 type sequence G description binding site for residue CL B 1001 source : AC3 13) chain B residue 484 type sequence F description binding site for residue CL B 1001 source : AC3 14) chain B residue 485 type sequence M description binding site for residue CL B 1001 source : AC3 15) chain B residue 189 type sequence S description binding site for residue CL B 1002 source : AC4 16) chain B residue 581 type sequence I description binding site for residue CL B 1002 source : AC4 17) chain A residue 180-183 type TOPO_DOM sequence HLIS description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 18) chain A residue 196-208 type TOPO_DOM sequence TILRGVVLKEYLT description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 19) chain A residue 247-268 type TOPO_DOM sequence SKFMYYSDILT description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 20) chain A residue 291-301 type TOPO_DOM sequence EVTSTYFAVRN description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 21) chain A residue 377-390 type TOPO_DOM sequence RKHKALSQFLAKHR description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 22) chain B residue 180-183 type TOPO_DOM sequence HLIS description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 23) chain B residue 196-208 type TOPO_DOM sequence TILRGVVLKEYLT description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 24) chain B residue 247-268 type TOPO_DOM sequence SKFMYYSDILT description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 25) chain B residue 291-301 type TOPO_DOM sequence EVTSTYFAVRN description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 26) chain B residue 377-390 type TOPO_DOM sequence RKHKALSQFLAKHR description Cytoplasmic => ECO:0000305 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 119-150 type TRANSMEM sequence IFLVLLGLLMALVSWSMDYVSAKSLQAYKWSY description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 28) chain A residue 159-179 type TRANSMEM sequence LQFLVWVTFPLVLILFSALFC description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 29) chain A residue 209-228 type TRANSMEM sequence MKAFVAKVVALTAGLGSGIP description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 30) chain A residue 229-246 type TRANSMEM sequence VGKEGPFVHIASICAAVL description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 31) chain A residue 302-321 type TRANSMEM sequence YWRGFFAATFSAFVFRVLAV description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 32) chain A residue 348-376 type TRANSMEM sequence LPAFAAIGICCGLLGAVFVYLHRQVMLGV description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 33) chain A residue 391-408 type TRANSMEM sequence LLYPGIVTFVIASFTFPP description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 458-478 type TRANSMEM sequence IIIFLFFVMKFWMSIVATTMP description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 479-498 type TRANSMEM sequence IPCGGFMPVFVLGAAFGRLV description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 558-578 type TRANSMEM sequence PMMVAVILANMVAQSLQPSLY description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 37) chain B residue 119-150 type TRANSMEM sequence IFLVLLGLLMALVSWSMDYVSAKSLQAYKWSY description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 38) chain B residue 159-179 type TRANSMEM sequence LQFLVWVTFPLVLILFSALFC description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 39) chain B residue 209-228 type TRANSMEM sequence MKAFVAKVVALTAGLGSGIP description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 40) chain B residue 229-246 type TRANSMEM sequence VGKEGPFVHIASICAAVL description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 41) chain B residue 302-321 type TRANSMEM sequence YWRGFFAATFSAFVFRVLAV description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 42) chain B residue 348-376 type TRANSMEM sequence LPAFAAIGICCGLLGAVFVYLHRQVMLGV description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 43) chain B residue 391-408 type TRANSMEM sequence LLYPGIVTFVIASFTFPP description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 44) chain B residue 458-478 type TRANSMEM sequence IIIFLFFVMKFWMSIVATTMP description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 45) chain B residue 479-498 type TRANSMEM sequence IPCGGFMPVFVLGAAFGRLV description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 46) chain B residue 558-578 type TRANSMEM sequence PMMVAVILANMVAQSLQPSLY description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI2 47) chain A residue 151-158 type TOPO_DOM sequence AQMQPSLP description Extracellular => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 48) chain A residue 322-347 type TOPO_DOM sequence WNKDAVTITALFRTNFRMDFPFDLKE description Extracellular => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 49) chain A residue 409-414 type TOPO_DOM sequence GMGQFM description Extracellular => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 50) chain A residue 427-457 type TOPO_DOM sequence LFDNNTWVKHAGDPESLGQSAVWIHPRVNVV description Extracellular => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 51) chain A residue 499-521 type TOPO_DOM sequence GEIMAMLFPDGILFDDIIYKILP description Extracellular => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 52) chain A residue 555-557 type TOPO_DOM sequence HIL description Extracellular => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 53) chain B residue 151-158 type TOPO_DOM sequence AQMQPSLP description Extracellular => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 54) chain B residue 322-347 type TOPO_DOM sequence WNKDAVTITALFRTNFRMDFPFDLKE description Extracellular => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 55) chain B residue 409-414 type TOPO_DOM sequence GMGQFM description Extracellular => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 56) chain B residue 427-457 type TOPO_DOM sequence LFDNNTWVKHAGDPESLGQSAVWIHPRVNVV description Extracellular => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 57) chain B residue 499-521 type TOPO_DOM sequence GEIMAMLFPDGILFDDIIYKILP description Extracellular => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 58) chain B residue 555-557 type TOPO_DOM sequence HIL description Extracellular => ECO:0000305 source Swiss-Prot : SWS_FT_FI3 59) chain A residue 184-195 type INTRAMEM sequence PQAVGSGIPEMK description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI4 60) chain A residue 269-290 type INTRAMEM sequence VGCAVGVGCCFGTPLGGVLFSI description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI4 61) chain A residue 415-426 type INTRAMEM sequence AGELMPREAIST description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI4 62) chain A residue 522-554 type INTRAMEM sequence GGYAVIGAAALTGAVSHTVSTAVICFELTGQIA description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI4 63) chain B residue 184-195 type INTRAMEM sequence PQAVGSGIPEMK description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI4 64) chain B residue 269-290 type INTRAMEM sequence VGCAVGVGCCFGTPLGGVLFSI description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI4 65) chain B residue 415-426 type INTRAMEM sequence AGELMPREAIST description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI4 66) chain B residue 522-554 type INTRAMEM sequence GGYAVIGAAALTGAVSHTVSTAVICFELTGQIA description Helical => ECO:0000269|PubMed:29809153 source Swiss-Prot : SWS_FT_FI4 67) chain B residue 484 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P37019 source Swiss-Prot : SWS_FT_FI5 68) chain B residue 578 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P37019 source Swiss-Prot : SWS_FT_FI5 69) chain A residue 484 type BINDING sequence F description BINDING => ECO:0000250|UniProtKB:P37019 source Swiss-Prot : SWS_FT_FI5 70) chain A residue 578 type BINDING sequence Y description BINDING => ECO:0000250|UniProtKB:P37019 source Swiss-Prot : SWS_FT_FI5 71) chain B residue 189 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P37019 source Swiss-Prot : SWS_FT_FI5 72) chain A residue 189 type BINDING sequence S description BINDING => ECO:0000250|UniProtKB:P37019 source Swiss-Prot : SWS_FT_FI5

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