eF-site ID 6gjq-ABCDEFGH PDB Code 6gjq Chain A, B, C, D, E, F, G, H click to enlarge Title human NBD1 of CFTR in complex with nanobody T27 Classification HYDROLASE Compound Cystic fibrosis transmembrane conductance regulator Source (6GJQ) Sequence A:  DINFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSRISF CPQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDI SKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL LDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHL KKADKILILHEGSSYFYGTFSELQNLQ B:  QVQLQESGGGLEQPGGSLRLSCATSGVIFGINAMGWYRQA PGKQRELVATFTSGGSTNYADFVEGRFTISRDNAKNTVYL QMNGLRPEDTAVYYCHATVVVSRYGLTYDYWGQGTQVTVS S C:  DINFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSRISF CPQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDI SKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL LDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHL KKADKILILHEGSSYFYGTFSELQNL D:  QVQLQESGGGLEQPGGSLRLSCATSGVIFGINAMGWYRQA PGKQRELVATFTSGGSTNYADFVEGRFTISRDNAKNTVYL QMNGLRPEDTAVYYCHATVVVSRYGLTYDYWGQGTQVTVS S E:  DINFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSRISF CPQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDI SKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL LDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHL KKADKILILHEGSSYFYGTFSELQNLQ F:  QVQLQESGGGLEQPGGSLRLSCATSGVIFGINAMGWYRQA PGKQRELVATFTSGGSTNYADFVEGRFTISRDNAKNTVYL QMNGLRPEDTAVYYCHATVVVSRYGLTYDYWGQGTQVTVS S G:  DINFKIERGQLLAVAGSTGAGKTSLLMMIMGELEPSRISF CPQFSWIMPGTIKENIIFGVSYDEYRYRSVIKACQLEEDI SKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYL LDSPFGYLDVLTEKEIFESCVCKLMANKTRILVTSKMEHL KKADKILILHEGSSYFYGTFSELQNLQ H:  QVQLQESGGGLEQPGGSLRLSCATSGVIFGINAMGWYRQA PGKQRELVATFTSGGSTNYADFVEGRFTISRDNAKNTVYL QMNGLRPEDTAVYYCHATVVVSRYGLTYDYWGQGTQVTVS S Description (1)  Cystic fibrosis transmembrane conductance regulator (E.C.3.6.3.49), Nanobody T27 Functional site 1) chain A residue 459 type sequence S description binding site for residue ATP A 701 source : AC1 2) chain A residue 460 type sequence T description binding site for residue ATP A 701 source : AC1 3) chain A residue 461 type sequence G description binding site for residue ATP A 701 source : AC1 4) chain A residue 462 type sequence A description binding site for residue ATP A 701 source : AC1 5) chain A residue 463 type sequence G description binding site for residue ATP A 701 source : AC1 6) chain A residue 464 type sequence K description binding site for residue ATP A 701 source : AC1 7) chain A residue 465 type sequence T description binding site for residue ATP A 701 source : AC1 8) chain A residue 466 type sequence S description binding site for residue ATP A 701 source : AC1 9) chain A residue 493 type sequence Q description binding site for residue ATP A 701 source : AC1 10) chain E residue 495 type sequence S description binding site for residue ATP A 701 source : AC1 11) chain C residue 460 type sequence T description binding site for residue ATP C 701 source : AC2 12) chain C residue 461 type sequence G description binding site for residue ATP C 701 source : AC2 13) chain C residue 462 type sequence A description binding site for residue ATP C 701 source : AC2 14) chain C residue 463 type sequence G description binding site for residue ATP C 701 source : AC2 15) chain C residue 464 type sequence K description binding site for residue ATP C 701 source : AC2 16) chain C residue 465 type sequence T description binding site for residue ATP C 701 source : AC2 17) chain C residue 466 type sequence S description binding site for residue ATP C 701 source : AC2 18) chain C residue 493 type sequence Q description binding site for residue ATP C 701 source : AC2 19) chain G residue 495 type sequence S description binding site for residue ATP C 701 source : AC2 20) chain A residue 494 type sequence F description binding site for residue ATP E 701 source : AC3 21) chain A residue 495 type sequence S description binding site for residue ATP E 701 source : AC3 22) chain E residue 443 type sequence D description binding site for residue ATP E 701 source : AC3 23) chain E residue 460 type sequence T description binding site for residue ATP E 701 source : AC3 24) chain E residue 461 type sequence G description binding site for residue ATP E 701 source : AC3 25) chain E residue 462 type sequence A description binding site for residue ATP E 701 source : AC3 26) chain E residue 463 type sequence G description binding site for residue ATP E 701 source : AC3 27) chain E residue 464 type sequence K description binding site for residue ATP E 701 source : AC3 28) chain E residue 465 type sequence T description binding site for residue ATP E 701 source : AC3 29) chain E residue 466 type sequence S description binding site for residue ATP E 701 source : AC3 30) chain E residue 493 type sequence Q description binding site for residue ATP E 701 source : AC3 31) chain C residue 494 type sequence F description binding site for residue ATP G 701 source : AC4 32) chain C residue 495 type sequence S description binding site for residue ATP G 701 source : AC4 33) chain C residue 496 type sequence W description binding site for residue ATP G 701 source : AC4 34) chain G residue 443 type sequence D description binding site for residue ATP G 701 source : AC4 35) chain G residue 460 type sequence T description binding site for residue ATP G 701 source : AC4 36) chain G residue 461 type sequence G description binding site for residue ATP G 701 source : AC4 37) chain G residue 462 type sequence A description binding site for residue ATP G 701 source : AC4 38) chain G residue 463 type sequence G description binding site for residue ATP G 701 source : AC4 39) chain G residue 464 type sequence K description binding site for residue ATP G 701 source : AC4 40) chain G residue 465 type sequence T description binding site for residue ATP G 701 source : AC4 41) chain G residue 466 type sequence S description binding site for residue ATP G 701 source : AC4 42) chain G residue 493 type sequence Q description binding site for residue ATP G 701 source : AC4 43) chain A residue 548-562 type prosite sequence LSGGQRARISLARAV description ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRARISLARAV source prosite : PS00211 44) chain A residue 549 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI5 45) chain C residue 549 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI5 46) chain E residue 549 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI5 47) chain G residue 549 type MOD_RES sequence S description Phosphoserine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI5 48) chain A residue 524 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:22119790 source Swiss-Prot : SWS_FT_FI6 49) chain C residue 524 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:22119790 source Swiss-Prot : SWS_FT_FI6 50) chain E residue 524 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:22119790 source Swiss-Prot : SWS_FT_FI6 51) chain G residue 524 type LIPID sequence C description S-palmitoyl cysteine => ECO:0000269|PubMed:22119790 source Swiss-Prot : SWS_FT_FI6 52) chain A residue 458 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0000269|PubMed:15528182, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:1XMJ, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS, ECO:0007744|PDB:2BBT source Swiss-Prot : SWS_FT_FI3 53) chain C residue 458 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0000269|PubMed:15528182, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:1XMJ, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS, ECO:0007744|PDB:2BBT source Swiss-Prot : SWS_FT_FI3 54) chain E residue 458 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0000269|PubMed:15528182, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:1XMJ, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS, ECO:0007744|PDB:2BBT source Swiss-Prot : SWS_FT_FI3 55) chain G residue 458 type BINDING sequence G description BINDING => ECO:0000255|PROSITE-ProRule:PRU00434, ECO:0000269|PubMed:15528182, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:1XMJ, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS, ECO:0007744|PDB:2BBT source Swiss-Prot : SWS_FT_FI3 56) chain A residue 493 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15528182, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS source Swiss-Prot : SWS_FT_FI4 57) chain C residue 493 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15528182, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS source Swiss-Prot : SWS_FT_FI4 58) chain E residue 493 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15528182, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS source Swiss-Prot : SWS_FT_FI4 59) chain G residue 493 type BINDING sequence Q description BINDING => ECO:0000269|PubMed:15528182, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS source Swiss-Prot : SWS_FT_FI4

Display surface Download Links