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SummaryStructural detailsExperimental detailsFunctional detailsSequence NeighborHistoryDownloads

9L0U

Cryo-EM structure of human lipid phosphate phosphatase 1 complexed with PO4.MAG

Functional Information from GO Data
ChainGOidnamespacecontents
A0000810molecular_functiondiacylglycerol diphosphate phosphatase activity
A0005515molecular_functionprotein binding
A0005886cellular_componentplasma membrane
A0005901cellular_componentcaveola
A0006644biological_processphospholipid metabolic process
A0006670biological_processsphingosine metabolic process
A0006672biological_processceramide metabolic process
A0007165biological_processsignal transduction
A0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
A0008195molecular_functionphosphatidate phosphatase activity
A0008285biological_processnegative regulation of cell population proliferation
A0016020cellular_componentmembrane
A0016324cellular_componentapical plasma membrane
A0019216biological_processregulation of lipid metabolic process
A0030149biological_processsphingolipid catabolic process
A0030518biological_processnuclear receptor-mediated steroid hormone signaling pathway
A0030521biological_processandrogen receptor signaling pathway
A0042392molecular_functionsphingosine-1-phosphate phosphatase activity
A0042577molecular_functionlipid phosphatase activity
A0045121cellular_componentmembrane raft
A0046839biological_processphospholipid dephosphorylation
A0052642molecular_functionlysophosphatidic acid phosphatase activity
A0070062cellular_componentextracellular exosome
A0106235molecular_functionceramide-1-phosphate phosphatase activity
B0000810molecular_functiondiacylglycerol diphosphate phosphatase activity
B0005515molecular_functionprotein binding
B0005886cellular_componentplasma membrane
B0005901cellular_componentcaveola
B0006644biological_processphospholipid metabolic process
B0006670biological_processsphingosine metabolic process
B0006672biological_processceramide metabolic process
B0007165biological_processsignal transduction
B0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
B0008195molecular_functionphosphatidate phosphatase activity
B0008285biological_processnegative regulation of cell population proliferation
B0016020cellular_componentmembrane
B0016324cellular_componentapical plasma membrane
B0019216biological_processregulation of lipid metabolic process
B0030149biological_processsphingolipid catabolic process
B0030518biological_processnuclear receptor-mediated steroid hormone signaling pathway
B0030521biological_processandrogen receptor signaling pathway
B0042392molecular_functionsphingosine-1-phosphate phosphatase activity
B0042577molecular_functionlipid phosphatase activity
B0045121cellular_componentmembrane raft
B0046839biological_processphospholipid dephosphorylation
B0052642molecular_functionlysophosphatidic acid phosphatase activity
B0070062cellular_componentextracellular exosome
B0106235molecular_functionceramide-1-phosphate phosphatase activity
C0000810molecular_functiondiacylglycerol diphosphate phosphatase activity
C0005515molecular_functionprotein binding
C0005886cellular_componentplasma membrane
C0005901cellular_componentcaveola
C0006644biological_processphospholipid metabolic process
C0006670biological_processsphingosine metabolic process
C0006672biological_processceramide metabolic process
C0007165biological_processsignal transduction
C0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
C0008195molecular_functionphosphatidate phosphatase activity
C0008285biological_processnegative regulation of cell population proliferation
C0016020cellular_componentmembrane
C0016324cellular_componentapical plasma membrane
C0019216biological_processregulation of lipid metabolic process
C0030149biological_processsphingolipid catabolic process
C0030518biological_processnuclear receptor-mediated steroid hormone signaling pathway
C0030521biological_processandrogen receptor signaling pathway
C0042392molecular_functionsphingosine-1-phosphate phosphatase activity
C0042577molecular_functionlipid phosphatase activity
C0045121cellular_componentmembrane raft
C0046839biological_processphospholipid dephosphorylation
C0052642molecular_functionlysophosphatidic acid phosphatase activity
C0070062cellular_componentextracellular exosome
C0106235molecular_functionceramide-1-phosphate phosphatase activity
D0000810molecular_functiondiacylglycerol diphosphate phosphatase activity
D0005515molecular_functionprotein binding
D0005886cellular_componentplasma membrane
D0005901cellular_componentcaveola
D0006644biological_processphospholipid metabolic process
D0006670biological_processsphingosine metabolic process
D0006672biological_processceramide metabolic process
D0007165biological_processsignal transduction
D0007200biological_processphospholipase C-activating G protein-coupled receptor signaling pathway
D0008195molecular_functionphosphatidate phosphatase activity
D0008285biological_processnegative regulation of cell population proliferation
D0016020cellular_componentmembrane
D0016324cellular_componentapical plasma membrane
D0019216biological_processregulation of lipid metabolic process
D0030149biological_processsphingolipid catabolic process
D0030518biological_processnuclear receptor-mediated steroid hormone signaling pathway
D0030521biological_processandrogen receptor signaling pathway
D0042392molecular_functionsphingosine-1-phosphate phosphatase activity
D0042577molecular_functionlipid phosphatase activity
D0045121cellular_componentmembrane raft
D0046839biological_processphospholipid dephosphorylation
D0052642molecular_functionlysophosphatidic acid phosphatase activity
D0070062cellular_componentextracellular exosome
D0106235molecular_functionceramide-1-phosphate phosphatase activity
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues480
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails
site_idSWS_FT_FI2
Number of Residues324
DetailsTopological domain: {"description":"Extracellular","evidences":[{"source":"UniProtKB","id":"Q61469","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI3
Number of Residues128
DetailsTopological domain: {"description":"Cytoplasmic","evidences":[{"source":"UniProtKB","id":"Q61469","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI4
Number of Residues32
DetailsRegion: {"description":"Phosphatase sequence motif I","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI5
Number of Residues12
DetailsRegion: {"description":"Phosphatase sequence motif II","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI6
Number of Residues44
DetailsRegion: {"description":"Phosphatase sequence motif III","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI7
Number of Residues8
DetailsMotif: {"description":"PDZ-binding; involved in localization to the apical cell membrane","evidences":[{"source":"PubMed","id":"14527693","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails
site_idSWS_FT_FI8
Number of Residues4
DetailsActive site: {"description":"Proton donors","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI9
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI10
Number of Residues4
DetailsSite: {"description":"Stabilizes the active site histidine for nucleophilic attack","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails
site_idSWS_FT_FI11
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

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PDB entries from 2026-03-25

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