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21NW

Cryo-EM structure of human Lipid Phosphate Phosphatase 2

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

253091

PDB entries from 2026-05-06

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