eF-site ID 6roj-AC
PDB Code 6roj
Chain A, C

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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
C:  TSKKPPNTAFRQQRLKAWQPILSPQSVLPLLIFVACIFTP
IGIGLIVSATKVQDLTIDYSHCDTKASTTAFEDIPKKYIK
YHFKSKVENKPQWRLTENENGEQSCELQFEIPNDIKKSIF
IYYKITNFYQNHRRYVQSFDTKQILGEPIKKDDLDTSCSP
IRSREDKIIYPCGLIANSMFNDTFSQVLSGIDDTEDYNLT
NKHISWSIDRHRFKTTKYNASDIVPPPNWMKKYPDGYTDE
NLPDIHTWEEFQVWMRTAAFPKFYKLTLKNESASLPKGKY
QMNIELNYPISLFGGTKSFVLTTNGAIGGRNMSLGVLYLI
VAGLCALFGIIFLVKLIFQP
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 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
2) chain A
residue 1065-1094
type TOPO_DOM
sequence DQFVSSRLLERYPQLYKLGQKGQFFSVYIF
description Cytoplasmic => ECO:0000255
source Swiss-Prot : SWS_FT_FI1
3) chain A
residue 1153-1161
type TOPO_DOM
sequence VTNQWTKFT
description Cytoplasmic => ECO:0000255
source Swiss-Prot : SWS_FT_FI1
4) chain C
residue 45-65
type TRANSMEM
sequence VLPLLIFVACIFTPIGIGLIV
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI2
5) chain A
residue 1203-1223
type TRANSMEM
sequence GVFWLTLIVLPIFALVRDFLW
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI2
6) chain C
residue 332-352
type TRANSMEM
sequence LGVLYLIVAGLCALFGIIFLV
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI2
7) chain A
residue 450-470
type TRANSMEM
sequence ALFTVLIVLILISSIGNVIMS
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI2
8) chain A
residue 491-511
type TRANSMEM
sequence FFKDFLTFWILFSNLVPISLF
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI2
9) chain A
residue 1013-1033
type TRANSMEM
sequence LYSFYKNTALYMTQFWYVFAN
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI2
10) chain A
residue 1044-1064
type TRANSMEM
sequence WTMSFYNLFFTVWPPFVIGVF
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI2
11) chain A
residue 1095-1115
type TRANSMEM
sequence WGWIINGFFHSAIVFIGTILI
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI2
12) chain A
residue 1132-1152
type TRANSMEM
sequence WSWGVTVYTTSVIIVLGKAAL
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI2
13) chain A
residue 1162-1182
type TRANSMEM
sequence LIAIPGSLLFWLIFFPIYASI
description Helical => ECO:0000255
source Swiss-Prot : SWS_FT_FI2
14) chain C
residue 66-331
type TOPO_DOM
sequence SATKVQDLTIDYSHCDTKASTTAFEDIPKKYIKYHFKSKV
ENKPQWRLTENENGEQSCELQFEIPNDIKKSIFIYYKITN
FYQNHRRYVQSFDTKQILGEPIKKDDLDTSCSPIRSREDK
IIYPCGLIANSMFNDTFSQVLSGIDDTEDYNLTNKHISWS
IDRHRFKTTKYNASDIVPPPNWMKKYPDGYTDENLPDIHT
WEEFQVWMRTAAFPKFYKLTLKNESASLPKGKYQMNIELN
YPISLFGGTKSFVLTTNGAIGGRNMS
description Lumenal => ECO:0000255
source Swiss-Prot : SWS_FT_FI3
15) chain A
residue 471-490
type TOPO_DOM
sequence TADAKHLSYLYLEGTNKAGL
description Lumenal => ECO:0000255
source Swiss-Prot : SWS_FT_FI3
16) chain A
residue 1034-1043
type TOPO_DOM
sequence AFSGQSIMES
description Lumenal => ECO:0000255
source Swiss-Prot : SWS_FT_FI3
17) chain A
residue 1116-1131
type TOPO_DOM
sequence YRYGFALNMHGELADH
description Lumenal => ECO:0000255
source Swiss-Prot : SWS_FT_FI3
18) chain A
residue 1183-1202
type TOPO_DOM
sequence FPHANISREYYGVVKHTYGS
description Lumenal => ECO:0000255
source Swiss-Prot : SWS_FT_FI3
19) chain A
residue 560-566
type prosite
sequence XKTGTLT
description ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
source prosite : PS00154
20) chain C
residue 329
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000255
source Swiss-Prot : SWS_FT_FI7
21) 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
22) chain A
residue 756
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:34023399, ECO:0007744|PDB:7OH5
source Swiss-Prot : SWS_FT_FI9
23) chain A
residue 835
type BINDING
sequence T
description BINDING => ECO:0000269|PubMed:34023399, ECO:0007744|PDB:7OH5
source Swiss-Prot : SWS_FT_FI9
24) chain A
residue 1149
type BINDING
sequence K
description BINDING => ECO:0000269|PubMed:34023399, ECO:0007744|PDB:7OH5
source Swiss-Prot : SWS_FT_FI9
25) chain A
residue 958
type BINDING
sequence D
description BINDING => ECO:0000250|UniProtKB:Q8NB49
source Swiss-Prot : SWS_FT_FI10
26) 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
27) 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
28) 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
29) 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
30) 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
31) 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
32) chain C
residue 199
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:31515475
source Swiss-Prot : SWS_FT_FI4
33) chain C
residue 288
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:31515475
source Swiss-Prot : SWS_FT_FI4
34) chain C
residue 216
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
35) 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
36) 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
37) 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
38) 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
39) 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
40) chain C
residue 237
type CARBOHYD
sequence N
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363
source Swiss-Prot : SWS_FT_FI6
41) chain A
residue 721
type CARBOHYD
sequence K
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363
source Swiss-Prot : SWS_FT_FI6
42) chain A
residue 755
type CARBOHYD
sequence R
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363
source Swiss-Prot : SWS_FT_FI6
43) chain A
residue 836
type CARBOHYD
sequence G
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363
source Swiss-Prot : SWS_FT_FI6
44) chain A
residue 837
type CARBOHYD
sequence D
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363
source Swiss-Prot : SWS_FT_FI6
45) chain A
residue 928
type CARBOHYD
sequence R
description N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363
source Swiss-Prot : SWS_FT_FI6
46) 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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