Summary Structural details Experimental details Functional details Sequence Neighbor History Downloads

7DSI

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

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000166	molecular_function	nucleotide binding
A	0000287	molecular_function	magnesium ion binding
A	0005215	molecular_function	transporter activity
A	0005515	molecular_function	protein binding
A	0005524	molecular_function	ATP binding
A	0005739	cellular_component	mitochondrion
A	0005783	cellular_component	endoplasmic reticulum
A	0005794	cellular_component	Golgi apparatus
A	0005886	cellular_component	plasma membrane
A	0005933	cellular_component	cellular bud
A	0005935	cellular_component	cellular bud neck
A	0006869	biological_process	lipid transport
A	0006886	biological_process	intracellular protein transport
A	0006897	biological_process	endocytosis
A	0007163	biological_process	establishment or maintenance of cell polarity
A	0010008	cellular_component	endosome membrane
A	0015914	biological_process	phospholipid transport
A	0016020	cellular_component	membrane
A	0016887	molecular_function	ATP hydrolysis activity
A	0030428	cellular_component	cell septum
A	0042802	molecular_function	identical protein binding
A	0045332	biological_process	phospholipid translocation
A	0046872	molecular_function	metal ion binding
A	0070867	cellular_component	mating projection tip membrane
A	0071944	cellular_component	cell periphery
A	0090554	molecular_function	phosphatidylcholine floppase activity
A	0090555	molecular_function	phosphatidylethanolamine flippase activity
A	0090556	molecular_function	phosphatidylserine floppase activity
A	0099040	biological_process	ceramide translocation
A	0140326	molecular_function	ATPase-coupled intramembrane lipid transporter activity
A	0140331	biological_process	aminophospholipid translocation
A	0140345	molecular_function	phosphatidylcholine flippase activity
A	0140346	molecular_function	phosphatidylserine flippase activity
A	0140351	molecular_function	glycosylceramide flippase activity
A	1990531	cellular_component	phospholipid-translocating ATPase complex
B	0005515	molecular_function	protein binding
B	0005737	cellular_component	cytoplasm
B	0005783	cellular_component	endoplasmic reticulum
B	0005794	cellular_component	Golgi apparatus
B	0005886	cellular_component	plasma membrane
B	0007166	biological_process	cell surface receptor signaling pathway
B	0015247	molecular_function	aminophospholipid flippase activity
B	0016020	cellular_component	membrane
B	0044088	biological_process	regulation of vacuole organization
B	0045332	biological_process	phospholipid translocation
B	0140331	biological_process	aminophospholipid translocation
B	0140345	molecular_function	phosphatidylcholine flippase activity
B	1990531	cellular_component	phospholipid-translocating ATPase complex

Functional Information from PROSITE/UniProt

site_id	PS00154
Number of Residues	7
Details	ATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT

Chain	Residue	Details
A	ASP667-THR673

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	65
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI2
Number of Residues	220
Details	Transmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI3
Number of Residues	606
Details	Topological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI4
Number of Residues	11
Details	Region: {"description":"Involved in phosphatidylcholine substrate selection","evidences":[{"source":"PubMed","id":"23302692","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI5
Number of Residues	1
Details	Active site: {"description":"4-aspartylphosphate intermediate","evidences":[{"source":"UniProtKB","id":"Q9Y2Q0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI6
Number of Residues	5
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9Y2Q0","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI7
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35294892","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSI","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI8
Number of Residues	2
Details	Binding site: {"evidences":[{"source":"PubMed","id":"33320091","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35294892","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7KYB","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI9
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"33320091","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"35294892","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7DSI","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7KYB","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7WHW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI10
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P39524","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI11
Number of Residues	3
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI12
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35294892","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSH","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI13
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"PubMed","id":"35294892","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7DSH","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"7WHW","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

site_id	SWS_FT_FI14
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"Q8NB49","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI15
Number of Residues	1
Details	Binding site: {"evidences":[{"source":"UniProtKB","id":"G0S196","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI16
Number of Residues	1
Details	Site: {"description":"Involved in the release of the transported lipid into the cytosolic leaflet","evidences":[{"source":"UniProtKB","id":"C7EXK4","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI17
Number of Residues	2
Details	Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"UniProtKB","id":"Q12675","evidenceCode":"ECO:0000250"}]}

Chain

Residue

Details

site_id	SWS_FT_FI18
Number of Residues	276
Details	Topological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

site_id	SWS_FT_FI19
Number of Residues	2
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

site_id	SWS_FT_FI20
Number of Residues	3
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"33320091","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

site_id	SWS_FT_FI21
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"33320091","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7KY5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

		Sequence (fasta)
		PDBx/mmCIF
		PDBML format (no-atom)
		PDB format (full)
		Validation report (PDF)