eF-site ID 2pzf-AB PDB Code 2pzf Chain A, B click to enlarge Title Minimal human CFTR first nucleotide binding domain as a head-to-tail dimer with delta F508 Classification HYDROLASE Compound Cystic fibrosis transmembrane conductance regulator Source (CFTR_HUMAN) Sequence A:  SLTTTEVVMENVTAFWGGTPVLKDINFKIERGQLLAVAGS TGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQFSWIMP GTIKENIIGVSYDEYRYRSVIKACQLEEDISKFAEKDNIV LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV LTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILH EGSSYFYGTFSELQNLDFSSKLMG B:  TTTEVVMENVTAFWEEGGTPVLKDINFKIERGQLLAVAGS TGAGKTSLLMMIMGELEPSEGKIKHSGRISFCSQFSWIMP GTIKENIIGVSYDEYRYRSVIKACQLEEDISKFAEKDNIV LGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDV LTEKEIFESCVCKLMANKTRILVTSKMEHLKKADKILILH EGSSYFYGTFSELQNL 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 B residue 465 type sequence T description BINDING SITE FOR RESIDUE MG B 4 source : AC2 4) chain B residue 493 type sequence Q description BINDING SITE FOR RESIDUE MG B 4 source : AC2 5) chain A residue 401 type sequence W description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 6) chain A residue 440 type sequence V description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 7) chain A residue 460 type sequence T description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 8) chain A residue 461 type sequence G description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 9) chain A residue 462 type sequence A description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 10) chain A residue 463 type sequence G description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 11) chain A residue 464 type sequence K description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 12) chain A residue 465 type sequence T description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 13) chain A residue 466 type sequence S description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 14) chain A residue 493 type sequence Q description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 15) chain B residue 533 type sequence F description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 16) chain B residue 547 type sequence T description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 17) chain B residue 549 type sequence S description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 18) chain B residue 550 type sequence G description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 19) chain B residue 551 type sequence G description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 20) chain B residue 552 type sequence Q description BINDING SITE FOR RESIDUE ATP A 1 source : AC3 21) chain A residue 547 type sequence T description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 22) chain A residue 549 type sequence S description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 23) chain A residue 550 type sequence G description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 24) chain A residue 551 type sequence G description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 25) chain A residue 552 type sequence Q description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 26) chain B residue 401 type sequence W description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 27) chain B residue 440 type sequence V description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 28) chain B residue 460 type sequence T description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 29) chain B residue 461 type sequence G description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 30) chain B residue 462 type sequence A description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 31) chain B residue 463 type sequence G description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 32) chain B residue 464 type sequence K description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 33) chain B residue 465 type sequence T description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 34) chain B residue 466 type sequence S description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 35) chain B residue 493 type sequence Q description BINDING SITE FOR RESIDUE ATP B 2 source : AC4 36) chain A residue 550 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI5 37) chain B residue 550 type MOD_RES sequence G description Phosphoserine => ECO:0007744|PubMed:20068231 source Swiss-Prot : SWS_FT_FI5 38) chain A residue 525 type LIPID sequence Q description S-palmitoyl cysteine => ECO:0000269|PubMed:22119790 source Swiss-Prot : SWS_FT_FI6 39) chain B residue 525 type LIPID sequence Q description S-palmitoyl cysteine => ECO:0000269|PubMed:22119790 source Swiss-Prot : SWS_FT_FI6 40) chain A residue 401 type BINDING sequence W description BINDING => ECO:0000269|PubMed:15528182, ECO:0000269|PubMed:20150177, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:1XMJ, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS, ECO:0007744|PDB:2BBT, ECO:0007744|PDB:2PZE, ECO:0007744|PDB:2PZF, ECO:0007744|PDB:2PZG source Swiss-Prot : SWS_FT_FI1 41) chain B residue 401 type BINDING sequence W description BINDING => ECO:0000269|PubMed:15528182, ECO:0000269|PubMed:20150177, ECO:0007744|PDB:1XMI, ECO:0007744|PDB:1XMJ, ECO:0007744|PDB:2BBO, ECO:0007744|PDB:2BBS, ECO:0007744|PDB:2BBT, ECO:0007744|PDB:2PZE, ECO:0007744|PDB:2PZF, ECO:0007744|PDB:2PZG source Swiss-Prot : SWS_FT_FI1 42) chain A residue 466 type BINDING sequence S description BINDING => ECO:0000269|PubMed:20150177, ECO:0007744|PDB:2PZE, ECO:0007744|PDB:2PZF, ECO:0007744|PDB:2PZG source Swiss-Prot : SWS_FT_FI2 43) chain B residue 466 type BINDING sequence S description BINDING => ECO:0000269|PubMed:20150177, ECO:0007744|PDB:2PZE, ECO:0007744|PDB:2PZF, ECO:0007744|PDB:2PZG source Swiss-Prot : SWS_FT_FI2 44) 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 45) chain B 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 46) 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 47) chain B 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 48) chain A residue 548-562 type prosite sequence LSGGQRARISLARAV description ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQRARISLARAV source prosite : PS00211

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