eF-site ID 6roj-A PDB Code 6roj Chain A click to enlarge Title Cryo-EM structure of the activated Drs2p-Cdc50p Classification LIPID TRANSPORT Compound Probable phospholipid-transporting ATPase DRS2,Oxaloacetate decarboxylase alpha chain Source (CDC50_YEAST) Sequence A:  PRVIHINDSLANSSFGYSDNHISTTKYNFATFLPKFLFQE FSKYANLFFLCTSAIQQVPHVSPTNRYTTIGTLLVVLIVS AMKECIEDIKRANSDKELNNSTAEIFSEAHDDFVEKRWID IRVGDIIRVKSEEPIPADTIILSSSEPEGLCYIETANLDG ETNLKIKQSRVETAKFIDVKTLKNMNGKVVSEQPNSSLYT YEGTMTLNDRQIPLSPDQMILRGATLRNTAWIFGLVIFTG HETKLLRNATATPIKRTAVEKIINRQIIALFTVLIVLILI SSIGNVIMSTADAKHLSYLYLEGTNKAGLFFKDFLTFWIL FSNLVPISLFVTVELIKYYQAFMIGSDLDLYYEKTDTPTV VRTSSLVEELGQIEYIFSXKTGTLTRNIMEFKSCSIAGHC YIDKIPEDKTATVEDGIEVGYRKFDDLKKKLNDPSDEDSP IINDFLTLLATCHTVIPEFQSDGSIKYQAASPDEGALVQG GADLGYKFIIRKPNSVTVLLEETGEEKEYQLLNICEFNST RKRMSAIFRFPDGSIKLFCKGADTVILERLDDEANQYVEA TMRHLEDYASEGLRTLCLAMRDISEGEYEEWNSIYNEAAT TLDNRAEKLDEAANLIEKNLILIGATAIEDKLQDGVPETI HTLQEAGIKIWVLTGDRQETAINIGMSCRLLSEDMNLLII NEETRDDTERNLLEKINALNEHQLSTHDMNTLALVIDGKS LGFALEPELEDYLLTVAKLCKAVICCRVSPLQKALVVKMV KRKSSSLLLAIGDGANDVSMIQAAHVGVGISGMEGMQAAR SADIAVGQFKFLKKLLLVHGSWSYQRISVAILYSFYKNTA LYMTQFWYVFANAFSGQSIMESWTMSFYNLFFTVWPPFVI GVFDQFVSSRLLERYPQLYKLGQKGQFFSVYIFWGWIING FFHSAIVFIGTILIYRYGFALNMHGELADHWSWGVTVYTT SVIIVLGKAALVTNQWTKFTLIAIPGSLLFWLIFFPIYAS IFPHANISREYYGVVKHTYGSGVFWLTLIVLPIFALVRDF LWKYYKRMYEPETYHVIQEMQKYN Description (1)  Probable phospholipid-transporting ATPase DRS2,Oxaloacetate decarboxylase alpha chain (E.C.7.6.2.1,7.2.4.2), Cell division control protein 50 Functional site 1) chain A residue 703 type BINDING sequence K description BINDING => ECO:0000269|PubMed:34023399, ECO:0007744|PDB:7OH5, ECO:0007744|PDB:7OH7 source Swiss-Prot : SWS_FT_FI8 2) chain A residue 756 type BINDING sequence T description BINDING => ECO:0000269|PubMed:34023399, ECO:0007744|PDB:7OH5 source Swiss-Prot : SWS_FT_FI9 3) chain A residue 835 type BINDING sequence T description BINDING => ECO:0000269|PubMed:34023399, ECO:0007744|PDB:7OH5 source Swiss-Prot : SWS_FT_FI9 4) chain A residue 1149 type BINDING sequence K description BINDING => ECO:0000269|PubMed:34023399, ECO:0007744|PDB:7OH5 source Swiss-Prot : SWS_FT_FI9 5) chain A residue 958 type BINDING sequence D description BINDING => ECO:0000250|UniProtKB:Q8NB49 source Swiss-Prot : SWS_FT_FI10 6) chain A residue 1219 type BINDING sequence R description BINDING => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:34023399, ECO:0007744|PDB:6ROI, ECO:0007744|PDB:7OH4, ECO:0007744|PDB:7OH5, ECO:0007744|PDB:7OH6 source Swiss-Prot : SWS_FT_FI11 7) chain A residue 1223 type BINDING sequence W description BINDING => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:34023399, ECO:0007744|PDB:6ROI, ECO:0007744|PDB:7OH4, ECO:0007744|PDB:7OH7 source Swiss-Prot : SWS_FT_FI12 8) chain A residue 1224 type BINDING sequence K description BINDING => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:34023399, ECO:0007744|PDB:6ROI, ECO:0007744|PDB:6ROJ, ECO:0007744|PDB:7OH4, ECO:0007744|PDB:7OH5, ECO:0007744|PDB:7OH6 source Swiss-Prot : SWS_FT_FI13 9) chain A residue 1235 type BINDING sequence Y description BINDING => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:34023399, ECO:0007744|PDB:6ROI, ECO:0007744|PDB:7OH7 source Swiss-Prot : SWS_FT_FI14 10) chain A residue 1236 type BINDING sequence H description BINDING => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:34023399, ECO:0007744|PDB:6ROI, ECO:0007744|PDB:6ROJ, ECO:0007744|PDB:7OH4, ECO:0007744|PDB:7OH5, ECO:0007744|PDB:7OH6, ECO:0007744|PDB:7OH7 source Swiss-Prot : SWS_FT_FI15 11) chain A residue 508 type SITE sequence I description Involved in the release of the transported lipid into the cytosolic leaflet => ECO:0000250|UniProtKB:C7EXK4 source Swiss-Prot : SWS_FT_FI16 12) chain A residue 560-566 type prosite sequence XKTGTLT description ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT source prosite : PS00154 13) chain A residue 512-1012 type TOPO_DOM sequence VTVELIKYYQAFMIGSDLDLYYEKTDTPTVVRTSSLVEEL GQIEYIFSXKTGTLTRNIMEFKSCSIAGHCYIDKIPEDKT ATVEDGIEVGYRKFDDLKKKLNDPSDEDSPIINDFLTLLA TCHTVIPEFQSDGSIKYQAASPDEGALVQGGADLGYKFII RKPNSVTVLLEETGEEKEYQLLNICEFNSTRKRMSAIFRF PDGSIKLFCKGADTVILERLDDEANQYVEATMRHLEDYAS EGLRTLCLAMRDISEGEYEEWNSIYNEAATTLDNRAEKLD EAANLIEKNLILIGATAIEDKLQDGVPETIHTLQEAGIKI WVLTGDRQETAINIGMSCRLLSEDMNLLIINEETRDDTER NLLEKINALNEHQLSTHDMNTLALVIDGKSLGFALEPELE DYLLTVAKLCKAVICCRVSPLQKALVVKMVKRKSSSLLLA IGDGANDVSMIQAAHVGVGISGMEGMQAARSADIAVGQFK FLKKLLLVHGSWSYQRISVAI description Cytoplasmic => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 14) chain A residue 1065-1094 type TOPO_DOM sequence DQFVSSRLLERYPQLYKLGQKGQFFSVYIF description Cytoplasmic => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 15) chain A residue 1153-1161 type TOPO_DOM sequence VTNQWTKFT description Cytoplasmic => ECO:0000255 source Swiss-Prot : SWS_FT_FI1 16) chain A residue 450-470 type TRANSMEM sequence ALFTVLIVLILISSIGNVIMS description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 17) chain A residue 491-511 type TRANSMEM sequence FFKDFLTFWILFSNLVPISLF description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 18) chain A residue 1013-1033 type TRANSMEM sequence LYSFYKNTALYMTQFWYVFAN description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 19) chain A residue 1044-1064 type TRANSMEM sequence WTMSFYNLFFTVWPPFVIGVF description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 20) chain A residue 1095-1115 type TRANSMEM sequence WGWIINGFFHSAIVFIGTILI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 21) chain A residue 1132-1152 type TRANSMEM sequence WSWGVTVYTTSVIIVLGKAAL description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 22) chain A residue 1162-1182 type TRANSMEM sequence LIAIPGSLLFWLIFFPIYASI description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 23) chain A residue 1203-1223 type TRANSMEM sequence GVFWLTLIVLPIFALVRDFLW description Helical => ECO:0000255 source Swiss-Prot : SWS_FT_FI2 24) chain A residue 471-490 type TOPO_DOM sequence TADAKHLSYLYLEGTNKAGL description Lumenal => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 25) chain A residue 1034-1043 type TOPO_DOM sequence AFSGQSIMES description Lumenal => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 26) chain A residue 1116-1131 type TOPO_DOM sequence YRYGFALNMHGELADH description Lumenal => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 27) chain A residue 1183-1202 type TOPO_DOM sequence FPHANISREYYGVVKHTYGS description Lumenal => ECO:0000255 source Swiss-Prot : SWS_FT_FI3 28) chain A residue 561 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:31515475, ECO:0007744|PDB:7OH6, ECO:0007744|PDB:7OH7 source Swiss-Prot : SWS_FT_FI5 29) chain A residue 562 type CARBOHYD sequence T description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:31515475, ECO:0007744|PDB:7OH6, ECO:0007744|PDB:7OH7 source Swiss-Prot : SWS_FT_FI5 30) chain A residue 698 type CARBOHYD sequence F description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:31515475, ECO:0007744|PDB:7OH6, ECO:0007744|PDB:7OH7 source Swiss-Prot : SWS_FT_FI5 31) chain A residue 954 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:31515475, ECO:0007744|PDB:7OH6, ECO:0007744|PDB:7OH7 source Swiss-Prot : SWS_FT_FI5 32) chain A residue 957 type CARBOHYD sequence N description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:31515475, ECO:0007744|PDB:7OH6, ECO:0007744|PDB:7OH7 source Swiss-Prot : SWS_FT_FI5 33) chain A residue 721 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363 source Swiss-Prot : SWS_FT_FI6 34) chain A residue 755 type CARBOHYD sequence R description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363 source Swiss-Prot : SWS_FT_FI6 35) chain A residue 836 type CARBOHYD sequence G description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363 source Swiss-Prot : SWS_FT_FI6 36) chain A residue 837 type CARBOHYD sequence D description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363 source Swiss-Prot : SWS_FT_FI6 37) chain A residue 928 type CARBOHYD sequence R description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363 source Swiss-Prot : SWS_FT_FI6 38) chain A residue 934 type CARBOHYD sequence K description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363 source Swiss-Prot : SWS_FT_FI6

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