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6ROJ

Cryo-EM structure of the activated Drs2p-Cdc50p

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005215molecular_functiontransporter activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005768cellular_componentendosome
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005802cellular_componenttrans-Golgi network
A0005886cellular_componentplasma membrane
A0006892biological_processpost-Golgi vesicle-mediated transport
A0006897biological_processendocytosis
A0008289molecular_functionlipid binding
A0010008cellular_componentendosome membrane
A0015914biological_processphospholipid transport
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0032456biological_processendocytic recycling
A0045332biological_processphospholipid translocation
A0046872molecular_functionmetal ion binding
A0070273molecular_functionphosphatidylinositol-4-phosphate binding
A0090555molecular_functionphosphatidylethanolamine flippase activity
A0090556molecular_functionphosphatidylserine floppase activity
A0140326molecular_functionATPase-coupled intramembrane lipid transporter activity
A0140331biological_processaminophospholipid translocation
A0140345molecular_functionphosphatidylcholine flippase activity
A0140346molecular_functionphosphatidylserine flippase activity
A1990530cellular_componentCdc50p-Drs2p complex
A1990531cellular_componentphospholipid-translocating ATPase complex
C0005515molecular_functionprotein binding
C0005768cellular_componentendosome
C0005783cellular_componentendoplasmic reticulum
C0005794cellular_componentGolgi apparatus
C0005802cellular_componenttrans-Golgi network
C0005829cellular_componentcytosol
C0005886cellular_componentplasma membrane
C0006886biological_processintracellular protein transport
C0006897biological_processendocytosis
C0015247molecular_functionaminophospholipid flippase activity
C0016020cellular_componentmembrane
C0031902cellular_componentlate endosome membrane
C0042147biological_processretrograde transport, endosome to Golgi
C0045332biological_processphospholipid translocation
C0051666biological_processactin cortical patch localization
C0140331biological_processaminophospholipid translocation
C1990530cellular_componentCdc50p-Drs2p complex
C1990531cellular_componentphospholipid-translocating ATPase complex
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
ABFD560-THR566

site_idPS00188
Number of Residues18
DetailsBIOTIN Biotin-requiring enzymes attachment site. GEvLliLeAMKMeteIrA
ChainResidueDetails
AGLY1424-ALA1441

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues81
DetailsTOPO_DOM: Cytoplasmic => ECO:0000255
ChainResidueDetails
CMET1-SER44
CLYS353-LEU391
AVAL512-ILE1012
AASP1065-PHE1094
AVAL1153-THR1161
ALYS1224-ASP1355

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
CVAL45-VAL65
CLEU332-VAL352
AALA450-SER470
APHE491-PHE511
ALEU1013-ASN1033
ATRP1044-PHE1064
ATRP1095-ILE1115
ATRP1132-LEU1152
ALEU1162-ILE1182
AGLY1203-TRP1223

site_idSWS_FT_FI3
Number of Residues265
DetailsTOPO_DOM: Lumenal => ECO:0000255
ChainResidueDetails
CSER66-SER331
ATHR471-LEU490
AALA1034-SER1043
ATYR1116-HIS1131
APHE1183-SER1202

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:31515475
ChainResidueDetails
CASN199
CASN288

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:31515475, ECO:0007744|PDB:7OH6, ECO:0007744|PDB:7OH7
ChainResidueDetails
ALYS561
ATHR562
APHE698
AASP954
AASN957
CASN216

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:31243363
ChainResidueDetails
ALYS721
AARG755
AGLY836
AASP837
AARG928
ALYS934
CASN237

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
CASN329

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:34023399, ECO:0007744|PDB:7OH5, ECO:0007744|PDB:7OH7
ChainResidueDetails
ALYS703

site_idSWS_FT_FI9
Number of Residues3
DetailsBINDING: BINDING => ECO:0000269|PubMed:34023399, ECO:0007744|PDB:7OH5
ChainResidueDetails
ATHR756
ATHR835
ALYS1149

site_idSWS_FT_FI10
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8NB49
ChainResidueDetails
AASP958

site_idSWS_FT_FI11
Number of Residues1
DetailsBINDING: 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
ChainResidueDetails
AARG1219

site_idSWS_FT_FI12
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:34023399, ECO:0007744|PDB:6ROI, ECO:0007744|PDB:7OH4, ECO:0007744|PDB:7OH7
ChainResidueDetails
ATRP1223

site_idSWS_FT_FI13
Number of Residues1
DetailsBINDING: 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
ChainResidueDetails
ALYS1224

site_idSWS_FT_FI14
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:31243363, ECO:0000269|PubMed:34023399, ECO:0007744|PDB:6ROI, ECO:0007744|PDB:7OH7
ChainResidueDetails
ATYR1235

site_idSWS_FT_FI15
Number of Residues1
DetailsBINDING: 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
ChainResidueDetails
AHIS1236

site_idSWS_FT_FI16
Number of Residues1
DetailsSITE: Involved in the release of the transported lipid into the cytosolic leaflet => ECO:0000250|UniProtKB:C7EXK4
ChainResidueDetails
AILE508

site_idSWS_FT_FI17
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER102

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: N6-biotinyllysine => ECO:0000250, ECO:0000255|PROSITE-ProRule:PRU01066
ChainResidueDetails
ALYS1434

218500

PDB entries from 2024-04-17

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