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7DSI

Cryo-EM structure of Dnf1 from Saccharomyces cerevisiae in yeast lipids with AMPPCP ( resting state )

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005215molecular_functiontransporter activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005739cellular_componentmitochondrion
A0005768cellular_componentendosome
A0005783cellular_componentendoplasmic reticulum
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0005933cellular_componentcellular bud
A0005935cellular_componentcellular bud neck
A0006869biological_processlipid transport
A0006886biological_processintracellular protein transport
A0006897biological_processendocytosis
A0007163biological_processestablishment or maintenance of cell polarity
A0010008cellular_componentendosome membrane
A0015914biological_processphospholipid transport
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0030428cellular_componentcell septum
A0042802molecular_functionidentical protein binding
A0045332biological_processphospholipid translocation
A0046872molecular_functionmetal ion binding
A0070867cellular_componentmating projection tip membrane
A0071944cellular_componentcell periphery
A0090554molecular_functionphosphatidylcholine floppase activity
A0090555molecular_functionphosphatidylethanolamine flippase activity
A0090556molecular_functionphosphatidylserine floppase activity
A0099040biological_processceramide translocation
A0140326molecular_functionATPase-coupled intramembrane lipid transporter activity
A0140331biological_processaminophospholipid translocation
A0140345molecular_functionphosphatidylcholine flippase activity
A0140346molecular_functionphosphatidylserine flippase activity
A0140351molecular_functionglycosylceramide flippase activity
A1990531cellular_componentphospholipid-translocating ATPase complex
B0005515molecular_functionprotein binding
B0005737cellular_componentcytoplasm
B0005783cellular_componentendoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0005886cellular_componentplasma membrane
B0007166biological_processcell surface receptor signaling pathway
B0015247molecular_functionaminophospholipid flippase activity
B0016020cellular_componentmembrane
B0044088biological_processregulation of vacuole organization
B0045332biological_processphospholipid translocation
B0140331biological_processaminophospholipid translocation
B0140345molecular_functionphosphatidylcholine flippase activity
B1990531cellular_componentphospholipid-translocating ATPase complex
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP667-THR673

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues93
DetailsTOPO_DOM: Cytoplasmic => ECO:0000305
ChainResidueDetails
BMET1-THR74
BTHR394-LYS414
ASER616-ILE1188
AASP1241-PHE1270
ALEU1329-TRP1334
AASP1397-ASN1571

site_idSWS_FT_FI2
Number of Residues40
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
BVAL75-ALA95
APRO1376-TYR1396
BPHE373-LEU393
AVAL554-TYR574
AALA595-ILE615
APRO1189-ASN1209
ATHR1220-LEU1240
ALEU1271-VAL1291
AARG1308-LEU1328
AASP1335-ILE1355

site_idSWS_FT_FI3
Number of Residues276
DetailsTOPO_DOM: Extracellular => ECO:0000305
ChainResidueDetails
BGLN96-PRO372
ATYR575-ALA594
AASP1210-TYR1219
ATYR1292-HIS1307
ATRP1356-ALA1375

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
BSER36

site_idSWS_FT_FI5
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
BASN113
BASN279
APHE842
AASP1130
AASN1133

site_idSWS_FT_FI6
Number of Residues3
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:33320091
ChainResidueDetails
BASN240
BASN298
BASN332

site_idSWS_FT_FI7
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:33320091, ECO:0007744|PDB:7KY5
ChainResidueDetails
BASN256
AARG1104

site_idSWS_FT_FI8
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:33320091, ECO:0000269|PubMed:35294892, ECO:0007744|PDB:7DSH, ECO:0007744|PDB:7DSI, ECO:0007744|PDB:7KYB, ECO:0007744|PDB:7WHW
ChainResidueDetails
ASER844

site_idSWS_FT_FI9
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P39524
ChainResidueDetails
ALYS847

site_idSWS_FT_FI10
Number of Residues3
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:P04191
ChainResidueDetails
ALYS871
AGLY990
AASP991

site_idSWS_FT_FI11
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:35294892, ECO:0007744|PDB:7DSH
ChainResidueDetails
ATHR910

site_idSWS_FT_FI12
Number of Residues1
DetailsBINDING: BINDING => ECO:0000269|PubMed:35294892, ECO:0007744|PDB:7DSH, ECO:0007744|PDB:7WHW
ChainResidueDetails
ATHR989

site_idSWS_FT_FI13
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q8NB49
ChainResidueDetails
AASP1134

site_idSWS_FT_FI14
Number of Residues1
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:G0S196
ChainResidueDetails
AARG1393

site_idSWS_FT_FI15
Number of Residues1
DetailsSITE: Involved in the release of the transported lipid into the cytosolic leaflet => ECO:0000250|UniProtKB:C7EXK4
ChainResidueDetails
AILE615

site_idSWS_FT_FI16
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER53

site_idSWS_FT_FI17
Number of Residues4
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ATHR70
ATHR94
ATHR109
ATHR1551

site_idSWS_FT_FI18
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER81

site_idSWS_FT_FI19
Number of Residues1
DetailsMOD_RES: Phosphothreonine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:19779198
ChainResidueDetails
ATHR85

site_idSWS_FT_FI20
Number of Residues5
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER92
ASER104
ASER365
ASER1552
ASER1563

site_idSWS_FT_FI21
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956
ChainResidueDetails
ASER351

site_idSWS_FT_FI22
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q12675
ChainResidueDetails
ASER354
ASER358

site_idSWS_FT_FI23
Number of Residues1
DetailsMOD_RES: Phosphotyrosine => ECO:0000250|UniProtKB:Q12675
ChainResidueDetails
ATYR368

site_idSWS_FT_FI24
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER1506

site_idSWS_FT_FI25
Number of Residues2
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0000250|UniProtKB:Q12675
ChainResidueDetails
ALYS895

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PDB entries from 2024-07-10

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