eF-site ID 4ayw-A PDB Code 4ayw Chain A click to enlarge Title STRUCTURE OF THE HUMAN MITOCHONDRIAL ABC TRANSPORTER, ABCB10 (PLATE FORM) Classification MEMBRANE PROTEIN Compound ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 10 Source Homo sapiens (Human) (ABCBA_HUMAN) Sequence A:  LPEARKLLGLAYPERRRLAAAVGFLTMSSVISMSAPFFLG KIIDVIYTNPTVDYSDNLTRLCLGLSAVFLCGAAANAIRV YLMQTSGQRIVNRLRTSLFSSILRQEVAFFDKTRTGELIN RLSSDTALLGRSVTENLSDGLRAGAQASVGISMMFFVSPN LATFVLSVVPPVSIIAVIYGRYLRKLTKVTQDSLAQATQL AEERIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAF ARAGFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELSS FLMYAFWVGISIGGLSSFYSELMKGLGAGGRLWELLEREP KLPFNEGVILNEKSFQGALEFKNVHFAYPARPEVPIFQDF SLSIPSGSVTALVGPSGSGKSTVLSLLLRLYDPASGTISL DGHDIRQLNPVWLRSKIGTVSQEPILFSCSIAENIAYGAD DPSSVTAEEIQRVAEVANAVAFIRNFPQGFNTVVGEKGVL LSGGQKQRIAIARALLKNPKILLLDELDAENEYLVQEALD RLMDGRTVLVIAHHLSTIKNANMVAVLDQGKITEYGKHEE Description (1)  ATP-BINDING CASSETTE SUB-FAMILY B MEMBER 10 Functional site 1) chain A residue 264 type sequence D description BINDING SITE FOR RESIDUE ANP A 1719 source : AC1 2) chain A residue 501 type sequence Y description BINDING SITE FOR RESIDUE ANP A 1719 source : AC1 3) chain A residue 529 type sequence S description BINDING SITE FOR RESIDUE ANP A 1719 source : AC1 4) chain A residue 530 type sequence G description BINDING SITE FOR RESIDUE ANP A 1719 source : AC1 5) chain A residue 532 type sequence G description BINDING SITE FOR RESIDUE ANP A 1719 source : AC1 6) chain A residue 533 type sequence K description BINDING SITE FOR RESIDUE ANP A 1719 source : AC1 7) chain A residue 534 type sequence S description BINDING SITE FOR RESIDUE ANP A 1719 source : AC1 8) chain A residue 535 type sequence T description BINDING SITE FOR RESIDUE ANP A 1719 source : AC1 9) chain A residue 416 type sequence K description BINDING SITE FOR RESIDUE LMT A 1724 source : AC2 10) chain A residue 419 type sequence L description BINDING SITE FOR RESIDUE LMT A 1724 source : AC2 11) chain A residue 677 type sequence D description BINDING SITE FOR RESIDUE LMT A 1724 source : AC2 12) chain A residue 678 type sequence R description BINDING SITE FOR RESIDUE LMT A 1724 source : AC2 13) chain A residue 681 type sequence D description BINDING SITE FOR RESIDUE LMT A 1724 source : AC2 14) chain A residue 170 type sequence R description BINDING SITE FOR RESIDUE Y01 A 1730 source : AC3 15) chain A residue 213 type sequence R description BINDING SITE FOR RESIDUE Y01 A 1730 source : AC3 16) chain A residue 227 type sequence A description BINDING SITE FOR RESIDUE Y01 A 1730 source : AC3 17) chain A residue 230 type sequence A description BINDING SITE FOR RESIDUE Y01 A 1730 source : AC3 18) chain A residue 234 type sequence Y description BINDING SITE FOR RESIDUE Y01 A 1730 source : AC3 19) chain A residue 235 type sequence L description BINDING SITE FOR RESIDUE Y01 A 1730 source : AC3 20) chain A residue 389 type sequence R description BINDING SITE FOR RESIDUE Y01 A 1730 source : AC3 21) chain A residue 393 type sequence F description BINDING SITE FOR RESIDUE Y01 A 1730 source : AC3 22) chain A residue 397 type sequence G description BINDING SITE FOR RESIDUE Y01 A 1730 source : AC3 23) chain A residue 404 type sequence L description BINDING SITE FOR RESIDUE Y01 A 1730 source : AC3 24) chain A residue 312-335 type TOPO_DOM sequence PNLATFVLSVVPPVSIIAVIYGRY description Mitochondrial matrix => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 454-527 type TOPO_DOM sequence ELMKGLGAGGRLWELLEREPKLPFNEGVILNEKSFQGALE FKNVHFAYPARPEVPIFQDFSLSIPSGSVTALVG description Mitochondrial matrix => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 226-290 type TOPO_DOM sequence AAANAIRVYLMQTSGQRIVNRLRTSLFSSILRQEVAFFDK TRTGELINRLSSDTALLGRSVTENL description Mitochondrial intermembrane => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 27) chain A residue 357-432 type TOPO_DOM sequence RIGNVRTVRAFGKEMTEIEKYASKVDHVMQLARKEAFARA GFFGATGLSGNLIVLSVLYKGGLLMGSAHMTVGELS description Mitochondrial intermembrane => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 28) chain A residue 549-550 type TOPO_DOM sequence GT description Mitochondrial intermembrane => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 29) chain A residue 634-648 type prosite sequence LSGGQKQRIAIARAL description ABC_TRANSPORTER_1 ABC transporters family signature. LSGGQKQRIAIARAL source prosite : PS00211 30) chain A residue 647 type BINDING sequence A description source Swiss-Prot : SWS_FT_FI4 31) chain A residue 385 type MOD_RES sequence M description N6-acetyllysine => ECO:0007744|PubMed:19608861 source Swiss-Prot : SWS_FT_FI5 32) chain A residue 702 type MOD_RES sequence A description S-glutathionyl cysteine => ECO:0000250|UniProtKB:Q9JI39 source Swiss-Prot : SWS_FT_FI6 33) chain A residue 291-311 type TRANSMEM sequence SDGLRAGAQASVGISMMFFVS description Helical => ECO:0000255|PROSITE-ProRule:PRU00441 source Swiss-Prot : SWS_FT_FI2 34) chain A residue 336-356 type TRANSMEM sequence LRKLTKVTQDSLAQATQLAEE description Helical => ECO:0000255|PROSITE-ProRule:PRU00441 source Swiss-Prot : SWS_FT_FI2 35) chain A residue 433-453 type TRANSMEM sequence SFLMYAFWVGISIGGLSSFYS description Helical => ECO:0000255|PROSITE-ProRule:PRU00441 source Swiss-Prot : SWS_FT_FI2 36) chain A residue 528-548 type TRANSMEM sequence PSGSGKSTVLSLLLRLYDPAS description Helical => ECO:0000255|PROSITE-ProRule:PRU00441 source Swiss-Prot : SWS_FT_FI2 37) chain A residue 551-571 type TRANSMEM sequence ISLDGHDIRQLNPVWLRSKIG description Helical => ECO:0000255|PROSITE-ProRule:PRU00441 source Swiss-Prot : SWS_FT_FI2

Display surface Download Links