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7RD6

Structure of the S. cerevisiae P4B ATPase lipid flippase in the E2P state

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0000166molecular_functionnucleotide binding
A0000287molecular_functionmagnesium ion binding
A0005215molecular_functiontransporter activity
A0005515molecular_functionprotein binding
A0005524molecular_functionATP binding
A0005737cellular_componentcytoplasm
A0005768cellular_componentendosome
A0005770cellular_componentlate endosome
A0005794cellular_componentGolgi apparatus
A0005802cellular_componenttrans-Golgi network
A0005886cellular_componentplasma membrane
A0006869biological_processlipid transport
A0006890biological_processretrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
A0006897biological_processendocytosis
A0007033biological_processvacuole organization
A0010008cellular_componentendosome membrane
A0015031biological_processprotein transport
A0015914biological_processphospholipid transport
A0016020cellular_componentmembrane
A0016887molecular_functionATP hydrolysis activity
A0045332biological_processphospholipid translocation
A0046872molecular_functionmetal ion binding
A0090555molecular_functionphosphatidylethanolamine flippase activity
A0090556molecular_functionphosphatidylserine floppase activity
A0098629biological_processtrans-Golgi network membrane organization
A0140326molecular_functionATPase-coupled intramembrane lipid transporter activity
A0140331biological_processaminophospholipid translocation
A0140346molecular_functionphosphatidylserine flippase activity
A0180013molecular_functionlysophosphatidylserine flippase activity
Functional Information from PROSITE/UniProt
site_idPS00154
Number of Residues7
DetailsATPASE_E1_E2 E1-E2 ATPases phosphorylation site. DKTGTLT
ChainResidueDetails
AASP503-THR509

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues220
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues62
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues21
DetailsTopological domain: {"description":"Extracellular","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsActive site: {"description":"4-aspartylphosphate intermediate","evidences":[{"evidenceCode":"ECO:0000305"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q9Y2Q0","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues8
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P04191","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P32660","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"34645814","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"7RD8","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI9
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"P39524","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI10
Number of Residues1
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q8NB49","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

242842

PDB entries from 2025-10-08

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