2Y6V

Peroxisomal alpha-beta-hydrolase Lpx1 (Yor084w) from Saccharomyces cerevisiae (crystal form I)

External Resource: Annotation

Domain Annotation: ECOD Classification
Domain Annotation: CATH
Protein Family Annotation
Gene Ontology: Gene Product Annotation
InterPro: Protein Family Classification
Protein Modification Annotation

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	PF12697	e2y6vA1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF12697	ECOD (1.6)
B	PF12697	e2y6vB1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF12697	ECOD (1.6)
C	PF12697	e2y6vC1	A: a/b three-layered sandwiches	X: alpha/beta-Hydrolases (From Topology)	H: alpha/beta-Hydrolases (From Topology)	T: alpha/beta-Hydrolases	F: PF12697	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
B	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)
C	3.40.50.1820	Alpha Beta	3-Layer(aba) Sandwich	Rossmann fold	Alpha/Beta hydrolase fold, catalytic domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A, B, C	PF12697	Alpha/beta hydrolase family (Abhydrolase_6)	Alpha/beta hydrolase family	This family contains alpha/beta hydrolase enzymes of diverse specificity.	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A, B, C	PEROXISOMAL MEMBRANE PROTEIN LPX1	hydrolase activity, acting on ester bonds carboxylic ester hydrolase activity triglyceride lipase activity hydrolase activity catalytic activity lipase activity	neutral lipid metabolic process lipid catabolic process catabolic process neutral lipid catabolic process cellular metabolic process glycerolipid catabolic process acylglycerol catabolic process primary metabolic process cellular lipid catabolic process cellular catabolic process triglyceride catabolic process organic substance metabolic process triglyceride metabolic process cellular lipid metabolic process neutral lipid metabolic process lipid catabolic process catabolic process neutral lipid catabolic process cellular metabolic process glycerolipid catabolic process acylglycerol catabolic process primary metabolic process cellular lipid catabolic process cellular catabolic process triglyceride catabolic process organic substance metabolic process triglyceride metabolic process cellular lipid metabolic process metabolic process cellular process glycerolipid metabolic process acylglycerol metabolic process organic substance catabolic process lipid metabolic process	peroxisomal matrix membrane-bounded organelle intracellular anatomical structure peroxisome membrane-enclosed lumen cellular anatomical entity intracellular membrane-bounded organelle intracellular organelle lumen intracellular organelle organelle lumen organelle microbody lumen microbody cytoplasm

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A, B, C	IPR000073	Alpha/beta hydrolase fold-1	Domain
A, B, C	IPR029058	Alpha/Beta hydrolase fold	Homologous Superfamily

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
A, B, C	CME	Parent Component: CYS
A, B, C	CSO	Parent Component: CYS RESID: AA0205 PSI-MOD : L-cysteine sulfenic acid MOD:00210

RCSB PDB Core Operations are funded by the U.S. National Science Foundation (DBI-2321666), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.