eF-site ID 1r10-AB PDB Code 1r10 Chain A, B click to enlarge Title Cystic fibrosis transmembrane conductance regulator (CFTR) nucleotide-binding domain one (NBD1) with ATP, I4122 space group Classification TRANSPORT PROTEIN Compound Cystic fibrosis transmembrane conductance regulator Source (CFTR_MOUSE) Sequence A:  GIIMENVTAFWEEGFGELLEKVSFSHLCLVGNPVLKNINL NIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG RVSFCSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQL QQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDA DLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVTSK MEHLRKADKILILHQGSSYFYGTFSELQSLRPDFSSKLMG YDTFDQFTEERRSSILTETLRRFS B:  GIIMENVTAFWEEGFGELLEKVSFSHLCLVGNPVLKNINL NIEKGEMLAITGSTGSGKTSLLMLILGELEASEGIIKHSG RVSFCSQFSWIMPGTIKENIIFGVSYDEYRYKSVVKACQL QQDITKFAEQDNTVLGEGGVTLSGGQRARISLARAVYKDA DLYLLDSPFGYLDVFTEEQVFESCVCKLMANKTRILVTSK MEHLRKADKILILHQGSSYFYGTFSELQSLRPDFSSKLMG YDTFDQFTEERRSSILTETLRRFS Description Functional site 1) chain A residue 465 type sequence T description BINDING SITE FOR RESIDUE MG A 3 source : AC1 2) chain A residue 493 type sequence Q description BINDING SITE FOR RESIDUE MG A 3 source : AC1 3) chain A residue 572 type sequence D description BINDING SITE FOR RESIDUE MG A 3 source : AC1 4) chain B residue 465 type sequence T description BINDING SITE FOR RESIDUE MG B 4 source : AC2 5) chain B residue 493 type sequence Q description BINDING SITE FOR RESIDUE MG B 4 source : AC2 6) chain B residue 572 type sequence D description BINDING SITE FOR RESIDUE MG B 4 source : AC2 7) chain A residue 401 type sequence W description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 8) chain A residue 409 type sequence L description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 9) chain A residue 430 type sequence F description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 10) chain A residue 461 type sequence G description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 11) chain A residue 462 type sequence S description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 12) chain A residue 463 type sequence G description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 13) chain A residue 464 type sequence K description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 14) chain A residue 465 type sequence T description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 15) chain A residue 466 type sequence S description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 16) chain B residue 498 type sequence M description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 17) chain B residue 401 type sequence W description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 18) chain B residue 410 type sequence E description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 19) chain B residue 460 type sequence T description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 20) chain B residue 461 type sequence G description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 21) chain B residue 462 type sequence S description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 22) chain B residue 463 type sequence G description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 23) chain B residue 464 type sequence K description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 24) chain B residue 465 type sequence T description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 25) chain B residue 466 type sequence S description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 26) chain B residue 493 type sequence Q description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 27) chain A residue 542 type sequence G description BINDING SITE FOR RESIDUE ACY A 7 source : AC5 28) chain A residue 545 type sequence G description BINDING SITE FOR RESIDUE ACY A 7 source : AC5 29) chain A residue 546 type sequence V description BINDING SITE FOR RESIDUE ACY A 7 source : AC5 30) chain A residue 547 type sequence T description BINDING SITE FOR RESIDUE ACY A 7 source : AC5 31) chain A residue 578 type sequence L description BINDING SITE FOR RESIDUE ACY B 8 source : AC6 32) chain B residue 541 type sequence L description BINDING SITE FOR RESIDUE ACY B 8 source : AC6 33) chain B residue 542 type sequence G description BINDING SITE FOR RESIDUE ACY B 8 source : AC6 34) chain B residue 545 type sequence G description BINDING SITE FOR RESIDUE ACY B 8 source : AC6 35) chain B residue 546 type sequence V description BINDING SITE FOR RESIDUE ACY B 8 source : AC6 36) chain B residue 547 type sequence T description BINDING SITE FOR RESIDUE ACY B 8 source : AC6 37) chain A residue 529 type sequence D description BINDING SITE FOR RESIDUE ACY A 9 source : AC7 38) chain A residue 532 type sequence K description BINDING SITE FOR RESIDUE ACY A 9 source : AC7 39) chain B residue 532 type sequence K description BINDING SITE FOR RESIDUE ACY A 9 source : AC7 40) chain B residue 552 type sequence Q description BINDING SITE FOR RESIDUE ACY A 9 source : AC7 41) chain A residue 524 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI6 42) chain B residue 524 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI6 43) chain A residue 670 type MOD_RES sequence S description Phosphoserine; by PKA => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI5 44) chain B residue 670 type MOD_RES sequence S description Phosphoserine; by PKA => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI5 45) chain A residue 548-562 type prosite sequence LSGGQRARISLARAV description ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRARISLARAV source prosite : PS00211 46) chain A residue 401 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI1 47) chain B residue 401 type BINDING sequence W description BINDING => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI1 48) chain A residue 549 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI4 49) chain A residue 660 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI4 50) chain B residue 549 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI4 51) chain B residue 660 type MOD_RES sequence S description Phosphoserine => ECO:0000250|UniProtKB:P13569 source Swiss-Prot : SWS_FT_FI4 52) 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 53) 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 54) 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 55) 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

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