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21NW

Cryo-EM structure of human Lipid Phosphate Phosphatase 2

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
A0005769cellular_componentearly endosome
A0005783cellular_componentendoplasmic reticulum
A0005789cellular_componentendoplasmic reticulum membrane
A0005886cellular_componentplasma membrane
A0005901cellular_componentcaveola
A0006644biological_processphospholipid metabolic process
A0006670biological_processsphingosine metabolic process
A0006672biological_processceramide metabolic process
A0007165biological_processsignal transduction
A0008195molecular_functionphosphatidate phosphatase activity
A0016020cellular_componentmembrane
A0030149biological_processsphingolipid catabolic process
A0031901cellular_componentearly endosome membrane
A0042392molecular_functionsphingosine-1-phosphate phosphatase activity
A0046839biological_processphospholipid dephosphorylation
A0106235molecular_functionceramide-1-phosphate phosphatase activity
B0005515molecular_functionprotein binding
B0005769cellular_componentearly endosome
B0005783cellular_componentendoplasmic reticulum
B0005789cellular_componentendoplasmic reticulum membrane
B0005886cellular_componentplasma membrane
B0005901cellular_componentcaveola
B0006644biological_processphospholipid metabolic process
B0006670biological_processsphingosine metabolic process
B0006672biological_processceramide metabolic process
B0007165biological_processsignal transduction
B0008195molecular_functionphosphatidate phosphatase activity
B0016020cellular_componentmembrane
B0030149biological_processsphingolipid catabolic process
B0031901cellular_componentearly endosome membrane
B0042392molecular_functionsphingosine-1-phosphate phosphatase activity
B0046839biological_processphospholipid dephosphorylation
B0106235molecular_functionceramide-1-phosphate phosphatase activity
C0005515molecular_functionprotein binding
C0005769cellular_componentearly endosome
C0005783cellular_componentendoplasmic reticulum
C0005789cellular_componentendoplasmic reticulum membrane
C0005886cellular_componentplasma membrane
C0005901cellular_componentcaveola
C0006644biological_processphospholipid metabolic process
C0006670biological_processsphingosine metabolic process
C0006672biological_processceramide metabolic process
C0007165biological_processsignal transduction
C0008195molecular_functionphosphatidate phosphatase activity
C0016020cellular_componentmembrane
C0030149biological_processsphingolipid catabolic process
C0031901cellular_componentearly endosome membrane
C0042392molecular_functionsphingosine-1-phosphate phosphatase activity
C0046839biological_processphospholipid dephosphorylation
C0106235molecular_functionceramide-1-phosphate phosphatase activity
D0005515molecular_functionprotein binding
D0005769cellular_componentearly endosome
D0005783cellular_componentendoplasmic reticulum
D0005789cellular_componentendoplasmic reticulum membrane
D0005886cellular_componentplasma membrane
D0005901cellular_componentcaveola
D0006644biological_processphospholipid metabolic process
D0006670biological_processsphingosine metabolic process
D0006672biological_processceramide metabolic process
D0007165biological_processsignal transduction
D0008195molecular_functionphosphatidate phosphatase activity
D0016020cellular_componentmembrane
D0030149biological_processsphingolipid catabolic process
D0031901cellular_componentearly endosome membrane
D0042392molecular_functionsphingosine-1-phosphate phosphatase activity
D0046839biological_processphospholipid dephosphorylation
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 Residues344
DetailsTopological domain: {"description":"Lumenal","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues32
DetailsRegion: {"description":"Phosphatase sequence motif I","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues12
DetailsRegion: {"description":"Phosphatase sequence motif II","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues44
DetailsRegion: {"description":"Phosphatase sequence motif III","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues4
DetailsActive site: {"description":"Proton donors","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues4
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"UniProtKB","id":"O34349","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI8
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_FI9
Number of Residues4
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

255615

PDB entries from 2026-06-24

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