Annotations: 3FGR

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2 Family	Phospholipase B-like	8046668	4005229	SCOP2 (2022-06-29)
A	SCOP2 Superfamily	Class II glutamine amidotransferases	8103582	3000131	SCOP2 (2022-06-29)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	2.10.70.60	Mainly Beta	Ribbon	Complement Module	domain 1	CATH (4.3.0)
A	1.10.439.20	Mainly Alpha	Orthogonal Bundle	Penicillin Amidohydrolase	domain 1	CATH (4.3.0)
B	3.60.60.20	Alpha Beta	4-Layer Sandwich	Penicillin V Acylase	Chain A	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF04916	Phospholipase B (Phospholip_B)	Phospholipase B	-	Family
B	PF04916	Phospholipase B (Phospholip_B)	Phospholipase B	-	Family

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	Putative phospholipase B-like 2 28 kDa form	hydrolase activity, acting on ester bonds carboxylic ester hydrolase activity hydrolase activity catalytic activity phospholipase activity lipase activity	lipid catabolic process catabolic process metabolic process cellular process primary metabolic process lipid metabolic process	membrane-bounded organelle intracellular anatomical structure lytic vacuole membrane-enclosed lumen vacuolar lumen vacuole intracellular membrane-bounded organelle lysosomal lumen intracellular organelle lumen intracellular organelle cellular anatomical structure organelle lumen organelle cytoplasm membrane-bounded organelle intracellular anatomical structure lytic vacuole membrane-enclosed lumen vacuolar lumen vacuole intracellular membrane-bounded organelle lysosomal lumen intracellular organelle lumen intracellular organelle cellular anatomical structure organelle lumen organelle cytoplasm lysosome
B	Putative phospholipase B-like 2 40 kDa form	hydrolase activity, acting on ester bonds carboxylic ester hydrolase activity hydrolase activity catalytic activity phospholipase activity lipase activity	lipid catabolic process catabolic process metabolic process cellular process primary metabolic process lipid metabolic process	membrane-bounded organelle intracellular anatomical structure lytic vacuole membrane-enclosed lumen vacuolar lumen vacuole intracellular membrane-bounded organelle lysosomal lumen intracellular organelle lumen intracellular organelle cellular anatomical structure organelle lumen organelle cytoplasm membrane-bounded organelle intracellular anatomical structure lytic vacuole membrane-enclosed lumen vacuolar lumen vacuole intracellular membrane-bounded organelle lysosomal lumen intracellular organelle lumen intracellular organelle cellular anatomical structure organelle lumen organelle cytoplasm lysosome

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR043042	Phospholipase B-like, domain 3	Homologous Superfamily
A	IPR043041	Phospholipase B-like, domain 2	Homologous Superfamily
A	IPR043040	Phospholipase B-like, domain 1	Homologous Superfamily
A	IPR007000	Phospholipase B-like	Family
B	IPR043042	Phospholipase B-like, domain 3	Homologous Superfamily
B	IPR043041	Phospholipase B-like, domain 2	Homologous Superfamily
B	IPR043040	Phospholipase B-like, domain 1	Homologous Superfamily
B	IPR007000	Phospholipase B-like	Family

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A, B	OPM	Monotopic/peripheral	Alpha + Beta monotopic/peripheral	NTN hydrolase superfamily	Phospholipase B

Protein Modification Annotation

Modified Residue(s)
Chain	Residue(s)	Description
B	OCS	Parent Component: CYS RESID: AA0556 PSI-MOD : L-cysteic acid (L-cysteine sulfonic acid) MOD:00460

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 R01GM157729.