eF-site ID 1r0x-ABCD PDB Code 1r0x Chain A, B, C, D click to enlarge Title Cystic fibrosis transmembrane conductance regulator (CFTR) nucleotide-binding domain one (NBD1) with ATP Classification TRANSPORT PROTEIN Compound Cystic fibrosis transmembrane conductance regulator Source (CFTR_MOUSE) Sequence A:  TGIIMENVTAFWEEGFGELLEKSFSHLCLVGNPVLKNINL NIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG RVSFCSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQL QQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDA DLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVTSK MEHLRKADKILILHQGSSYFYGTFSELQSLRPDFSSKLMG YDTFDQFTEERRSSILTETLRRFS B:  TTGIIMENVTAFWEEGFGELLEKSFSHLCLVGNPVLKNIN LNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHS GRVSFCSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQ LQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKD ADLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVTS KMEHLRKADKILILHQGSSYFYGTFSELQSLRPDFSSKLM GYDTFDQFTEERRSSILTETLRRFS C:  STTGIIMENVTAFWEEGFGELLEKFSHLCLVGNPVLKNIN LNIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHS GRVSFCSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQ LQQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKD ADLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVTS KMEHLRKADKILILHQGSSYFYGTFSELQSLRPDFSSKLM GYDTFDQFTEERRSSILTETLRRFS D:  TGIIMENVTAFWEEGFGELLEKFSHLCLVGNPVLKNINLN IEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSGR VSFCSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQLQ QDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDAD LYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVTSKM EHLRKADKILILHQGSSYFYGTFSELQSLRPDFSSKLMGY DTFDQFTEERRSSILTETLRRFS Description Functional site 1) chain B residue 465 type sequence T description BINDING SITE FOR RESIDUE MG B 11 source : AC1 2) chain B residue 493 type sequence Q description BINDING SITE FOR RESIDUE MG B 11 source : AC1 3) chain C residue 465 type sequence T description BINDING SITE FOR RESIDUE MG C 12 source : AC2 4) chain C residue 493 type sequence Q description BINDING SITE FOR RESIDUE MG C 12 source : AC2 5) chain A residue 465 type sequence T description BINDING SITE FOR RESIDUE MG A 13 source : AC3 6) chain A residue 493 type sequence Q description BINDING SITE FOR RESIDUE MG A 13 source : AC3 7) chain D residue 465 type sequence T description BINDING SITE FOR RESIDUE MG D 14 source : AC4 8) chain D residue 493 type sequence Q description BINDING SITE FOR RESIDUE MG D 14 source : AC4 9) chain A residue 401 type sequence W description BINDING SITE FOR RESIDUE ATP A 1 source : AC5 10) chain A residue 409 type sequence L description BINDING SITE FOR RESIDUE ATP A 1 source : AC5 11) chain A residue 430 type sequence F description BINDING SITE FOR RESIDUE ATP A 1 source : AC5 12) chain A residue 460 type sequence T description BINDING SITE FOR RESIDUE ATP A 1 source : AC5 13) chain A residue 461 type sequence G description BINDING SITE FOR RESIDUE ATP A 1 source : AC5 14) chain A residue 462 type sequence S description BINDING SITE FOR RESIDUE ATP A 1 source : AC5 15) chain A residue 463 type sequence G description BINDING SITE FOR RESIDUE ATP A 1 source : AC5 16) chain A residue 464 type sequence K description BINDING SITE FOR RESIDUE ATP A 1 source : AC5 17) chain A residue 465 type sequence T description BINDING SITE FOR RESIDUE ATP A 1 source : AC5 18) chain A residue 466 type sequence S description BINDING SITE FOR RESIDUE ATP A 1 source : AC5 19) chain A residue 493 type sequence Q description BINDING SITE FOR RESIDUE ATP A 1 source : AC5 20) chain B residue 498 type sequence M description BINDING SITE FOR RESIDUE ATP A 1 source : AC5 21) chain B residue 401 type sequence W description BINDING SITE FOR RESIDUE ATP B 2 source : AC6 22) chain B residue 410 type sequence E description BINDING SITE FOR RESIDUE ATP B 2 source : AC6 23) chain B residue 430 type sequence F description BINDING SITE FOR RESIDUE ATP B 2 source : AC6 24) chain B residue 460 type sequence T description BINDING SITE FOR RESIDUE ATP B 2 source : AC6 25) chain B residue 461 type sequence G description BINDING SITE FOR RESIDUE ATP B 2 source : AC6 26) chain B residue 462 type sequence S description BINDING SITE FOR RESIDUE ATP B 2 source : AC6 27) chain B residue 463 type sequence G description BINDING SITE FOR RESIDUE ATP B 2 source : AC6 28) chain B residue 464 type sequence K description BINDING SITE FOR RESIDUE ATP B 2 source : AC6 29) chain B residue 465 type sequence T description BINDING SITE FOR RESIDUE ATP B 2 source : AC6 30) chain B residue 466 type sequence S description BINDING SITE FOR RESIDUE ATP B 2 source : AC6 31) chain B residue 493 type sequence Q description BINDING SITE FOR RESIDUE ATP B 2 source : AC6 32) chain C residue 401 type sequence W description BINDING SITE FOR RESIDUE ATP C 3 source : AC7 33) chain C residue 409 type sequence L description BINDING SITE FOR RESIDUE ATP C 3 source : AC7 34) chain C residue 430 type sequence F description BINDING SITE FOR RESIDUE ATP C 3 source : AC7 35) chain C residue 460 type sequence T description BINDING SITE FOR RESIDUE ATP C 3 source : AC7 36) chain C residue 461 type sequence G description BINDING SITE FOR RESIDUE ATP C 3 source : AC7 37) chain C residue 462 type sequence S description BINDING SITE FOR RESIDUE ATP C 3 source : AC7 38) chain C residue 463 type sequence G description BINDING SITE FOR RESIDUE ATP C 3 source : AC7 39) chain C residue 464 type sequence K description BINDING SITE FOR RESIDUE ATP C 3 source : AC7 40) chain C residue 465 type sequence T description BINDING SITE FOR RESIDUE ATP C 3 source : AC7 41) chain C residue 466 type sequence S description BINDING SITE FOR RESIDUE ATP C 3 source : AC7 42) chain C residue 493 type sequence Q description BINDING SITE FOR RESIDUE ATP C 3 source : AC7 43) chain D residue 401 type sequence W description BINDING SITE FOR RESIDUE ATP D 4 source : AC8 44) chain D residue 409 type sequence L description BINDING SITE FOR RESIDUE ATP D 4 source : AC8 45) chain D residue 460 type sequence T description BINDING SITE FOR RESIDUE ATP D 4 source : AC8 46) chain D residue 461 type sequence G description BINDING SITE FOR RESIDUE ATP D 4 source : AC8 47) chain D residue 462 type sequence S description BINDING SITE FOR RESIDUE ATP D 4 source : AC8 48) chain D residue 463 type sequence G description BINDING SITE FOR RESIDUE ATP D 4 source : AC8 49) chain D residue 464 type sequence K description BINDING SITE FOR RESIDUE ATP D 4 source : AC8 50) chain D residue 465 type sequence T description BINDING SITE FOR RESIDUE ATP D 4 source : AC8 51) chain D residue 466 type sequence S description BINDING SITE FOR RESIDUE ATP D 4 source : AC8 52) chain D residue 493 type sequence Q description BINDING SITE FOR RESIDUE ATP D 4 source : AC8 53) chain A residue 541 type sequence L description BINDING SITE FOR RESIDUE ACY A 5 source : AC9 54) chain A residue 542 type sequence G description BINDING SITE FOR RESIDUE ACY A 5 source : AC9 55) chain A residue 545 type sequence G description BINDING SITE FOR RESIDUE ACY A 5 source : AC9 56) chain A residue 546 type sequence V description BINDING SITE FOR RESIDUE ACY A 5 source : AC9 57) chain A residue 547 type sequence T description BINDING SITE FOR RESIDUE ACY A 5 source : AC9 58) chain B residue 578 type sequence L description BINDING SITE FOR RESIDUE ACY A 5 source : AC9 59) chain B residue 542 type sequence G description BINDING SITE FOR RESIDUE ACY B 6 source : BC1 60) chain B residue 545 type sequence G description BINDING SITE FOR RESIDUE ACY B 6 source : BC1 61) chain B residue 546 type sequence V description BINDING SITE FOR RESIDUE ACY B 6 source : BC1 62) chain B residue 547 type sequence T description BINDING SITE FOR RESIDUE ACY B 6 source : BC1 63) chain C residue 541 type sequence L description BINDING SITE FOR RESIDUE ACY C 7 source : BC2 64) chain C residue 542 type sequence G description BINDING SITE FOR RESIDUE ACY C 7 source : BC2 65) chain C residue 545 type sequence G description BINDING SITE FOR RESIDUE ACY C 7 source : BC2 66) chain C residue 546 type sequence V description BINDING SITE FOR RESIDUE ACY C 7 source : BC2 67) chain C residue 547 type sequence T description BINDING SITE FOR RESIDUE ACY C 7 source : BC2 68) chain D residue 578 type sequence L description BINDING SITE FOR RESIDUE ACY C 7 source : BC2 69) chain D residue 540 type sequence V description BINDING SITE FOR RESIDUE ACY D 8 source : BC3 70) chain D residue 541 type sequence L description BINDING SITE FOR RESIDUE ACY D 8 source : BC3 71) chain D residue 542 type sequence G description BINDING SITE FOR RESIDUE ACY D 8 source : BC3 72) chain D residue 545 type sequence G description BINDING SITE FOR RESIDUE ACY D 8 source : BC3 73) chain D residue 546 type sequence V description BINDING SITE FOR RESIDUE ACY D 8 source : BC3 74) chain D residue 547 type sequence T description BINDING SITE FOR RESIDUE ACY D 8 source : BC3 75) chain C residue 532 type sequence K description BINDING SITE FOR RESIDUE ACY D 9 source : BC4 76) chain C residue 552 type sequence Q description BINDING SITE FOR RESIDUE ACY D 9 source : BC4 77) chain D residue 532 type sequence K description BINDING SITE FOR RESIDUE ACY D 9 source : BC4 78) chain D residue 549 type sequence S description BINDING SITE FOR RESIDUE ACY D 9 source : BC4 79) chain D residue 552 type sequence Q description BINDING SITE FOR RESIDUE ACY D 9 source : BC4 80) chain A residue 532 type sequence K description BINDING SITE FOR RESIDUE ACY A 10 source : BC5 81) chain A residue 549 type sequence S description BINDING SITE FOR RESIDUE ACY A 10 source : BC5 82) chain A residue 552 type sequence Q description BINDING SITE FOR RESIDUE ACY A 10 source : BC5 83) chain B residue 532 type sequence K description BINDING SITE FOR RESIDUE ACY A 10 source : BC5 84) chain A residue 524 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI6 85) chain B residue 524 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI6 86) chain C residue 524 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI6 87) chain D residue 524 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI6 88) chain A residue 670 type MOD_RES sequence S description Phosphoserine; by PKA => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI5 89) chain B residue 670 type MOD_RES sequence S description Phosphoserine; by PKA => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI5 90) chain C residue 670 type MOD_RES sequence S description Phosphoserine; by PKA => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI5 91) chain D residue 670 type MOD_RES sequence S description Phosphoserine; by PKA => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI5 92) chain A residue 401 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI1 93) chain B residue 401 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI1 94) chain C residue 401 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI1 95) chain D residue 401 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI1 96) chain A residue 493 type BINDING sequence Q description BINDING => ECO:0007744|PDB:1Q3H, ECO:0007744|PDB:1R0X, ECO:0007744|PDB:1R0Z, ECO:0007744|PDB:1XFA source Swiss-Prot : SWS_FT_FI3 97) chain B residue 493 type BINDING sequence Q description BINDING => ECO:0007744|PDB:1Q3H, ECO:0007744|PDB:1R0X, ECO:0007744|PDB:1R0Z, ECO:0007744|PDB:1XFA source Swiss-Prot : SWS_FT_FI3 98) chain C residue 493 type BINDING sequence Q description BINDING => ECO:0007744|PDB:1Q3H, ECO:0007744|PDB:1R0X, ECO:0007744|PDB:1R0Z, ECO:0007744|PDB:1XFA source Swiss-Prot : SWS_FT_FI3 99) chain D residue 493 type BINDING sequence Q description BINDING => ECO:0007744|PDB:1Q3H, ECO:0007744|PDB:1R0X, ECO:0007744|PDB:1R0Z, ECO:0007744|PDB:1XFA source Swiss-Prot : SWS_FT_FI3 100) chain A residue 548-562 type prosite sequence LSGGQRARISLARAV description ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRARISLARAV source prosite : PS00211 101) chain A residue 458 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0007744|PDB:1Q3H, ECO:0007744|PDB:1R0X, ECO:0007744|PDB:1R0Z, ECO:0007744|PDB:1R10, ECO:0007744|PDB:1XF9, ECO:0007744|PDB:1XFA, ECO:0007744|PDB:3SI7 source Swiss-Prot : SWS_FT_FI2 102) chain B residue 458 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0007744|PDB:1Q3H, ECO:0007744|PDB:1R0X, ECO:0007744|PDB:1R0Z, ECO:0007744|PDB:1R10, ECO:0007744|PDB:1XF9, ECO:0007744|PDB:1XFA, ECO:0007744|PDB:3SI7 source Swiss-Prot : SWS_FT_FI2 103) chain C residue 458 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0007744|PDB:1Q3H, ECO:0007744|PDB:1R0X, ECO:0007744|PDB:1R0Z, ECO:0007744|PDB:1R10, ECO:0007744|PDB:1XF9, ECO:0007744|PDB:1XFA, ECO:0007744|PDB:3SI7 source Swiss-Prot : SWS_FT_FI2 104) chain D residue 458 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0007744|PDB:1Q3H, ECO:0007744|PDB:1R0X, ECO:0007744|PDB:1R0Z, ECO:0007744|PDB:1R10, ECO:0007744|PDB:1XF9, ECO:0007744|PDB:1XFA, ECO:0007744|PDB:3SI7 source Swiss-Prot : SWS_FT_FI2 105) chain A residue 549 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI4 106) chain A residue 660 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI4 107) chain B residue 549 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI4 108) chain B residue 660 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI4 109) chain C residue 549 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI4 110) chain C residue 660 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI4 111) chain D residue 549 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI4 112) chain D residue 660 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI4

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