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3UUE

Crystal structure of mono- and diacylglycerol lipase from Malassezia globosa

Functional Information from GO Data
ChainGOidnamespacecontents
A0005576cellular_componentextracellular region
A0006629biological_processlipid metabolic process
A0016042biological_processlipid catabolic process
A0016787molecular_functionhydrolase activity
A0046872molecular_functionmetal ion binding
Functional Information from PROSITE/UniProt
site_idPS00120
Number of Residues10
DetailsLIPASE_SER Lipases, serine active site. VTVIGHSLGA
ChainResidueDetails
AVAL165-ALA174

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU10037","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22484238","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3UUE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UUF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"evidences":[{"source":"PubMed","id":"22484238","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3UUE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UUF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues1
DetailsGlycosylation: {"description":"O-linked (Man...) threonine","evidences":[{"source":"PubMed","id":"22484238","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3UUE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UUF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues1
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PROSITE-ProRule","id":"PRU00498","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"22484238","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"3UUE","evidenceCode":"ECO:0007744"},{"source":"PDB","id":"3UUF","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239149

PDB entries from 2025-07-23

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