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6LCR

Cryo-EM structure of Dnf1 from Chaetomium thermophilum in the E1-ATP state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005215molecular_functiontransporter activity
A0005524molecular_functionATP binding
A0005768cellular_componentendosome
A0005794cellular_componentGolgi apparatus
A0005886cellular_componentplasma membrane
A0006869biological_processlipid transport
A0006897biological_processendocytosis
A0007163biological_processestablishment or maintenance of cell polarity
A0010008cellular_componentendosome membrane
A0015914biological_processphospholipid transport
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0045332biological_processphospholipid translocation
A0046872molecular_functionmetal ion binding
A0070867cellular_componentmating projection tip membrane
A0090554molecular_functionphosphatidylcholine floppase activity
A0090556molecular_functionphosphatidylserine floppase activity
A0099040biological_processceramide translocation
A0140326molecular_functionATPase-coupled intramembrane lipid transporter activity
A0140331biological_processaminophospholipid translocation
A0140346molecular_functionphosphatidylserine flippase activity
A0140351molecular_functionglycosylceramide flippase activity
A1990531cellular_componentphospholipid-translocating ATPase complex
B0005783cellular_componentendoplasmic reticulum
B0005794cellular_componentGolgi apparatus
B0005886cellular_componentplasma membrane
B0016020cellular_componentmembrane
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP606-THR612

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues200
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues347
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues599
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"UniProtKB","id":"Q9Y2Q0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues5
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9Y2Q0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P32660","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P39524","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues3
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q8NB49","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"32303992","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6LCP","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI11
Number of Residues1
DetailsSite: {"description":"Involved in the release of the transported lipid into the cytosolic leaflet","evidences":[{"source":"UniProtKB","id":"C7EXK4","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI12
Number of Residues6
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

238895

PDB entries from 2025-07-16

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