Annotations: 1KP4

Domain Annotation: SCOP/SCOPe Classification SCOP-e Database Homepage

Chains	Domain Info	Class	Fold	Superfamily	Family	Domain	Species	Provenance Source (Version)
A	d1kp4a_	All alpha proteins	Phospholipase A2, PLA2	Phospholipase A2, PLA2	Prokaryotic phospholipase A2	Prokaryotic phospholipase A2	(Streptomyces violaceoruber ) [TaxId: 1935 ],	SCOPe (2.08)

Domain Annotation: SCOP2 Classification SCOP2 Database Homepage

Chains	Type	Family Name	Domain Identifier	Family Identifier	Provenance Source (Version)
A	SCOP2B Superfamily	Phospholipase A2, PLA2	8033015	3001690	SCOP2B (2022-06-29)

Domain Annotation: ECOD Classification ECOD Database Homepage

Chains	Family Name	Domain Identifier	Architecture	Possible Homology	Homology	Topology	Family	Provenance Source (Version)
A	Phospholip_A2_3	e1kp4A1	A: few secondary structure elements	X: Phospholipase A2, PLA2 (From Topology)	H: Phospholipase A2, PLA2 (From Topology)	T: Phospholipase A2, PLA2	F: Phospholip_A2_3	ECOD (1.6)

Domain Annotation: CATH CATH Database Homepage

Chain	Domain	Class	Architecture	Topology	Homology	Provenance Source (Version)
A	1.20.90.10	Mainly Alpha	Up-down Bundle	Phospholipase A2	Phospholipase A2 domain	CATH (4.3.0)

Protein Family Annotation Pfam Database Homepage

Chains	Accession	Name	Description	Comments	Source
A	PF09056	Prokaryotic phospholipase A2 (Phospholip_A2_3)	Prokaryotic phospholipase A2	The prokaryotic phospholipase A2 domain is predominantly found in bacterial and fungal phospholipases, as well as various hypothetical and putative proteins. It enables the liberation of fatty acids and lysophospholipid by hydrolysing the 2-ester bon ...	The prokaryotic phospholipase A2 domain is predominantly found in bacterial and fungal phospholipases, as well as various hypothetical and putative proteins. It enables the liberation of fatty acids and lysophospholipid by hydrolysing the 2-ester bond of 1,2-diacyl-3-sn-phosphoglycerides. The domain adopts an alpha-helical secondary structure, consisting of five alpha-helices and two helical segments [1].	Domain

Gene Ontology: Gene Product Annotation Gene Ontology Database Homepage

Chains	Polymer	Molecular Function	Biological Process	Cellular Component
A	phospholipase A2	phospholipase A2 activity hydrolase activity, acting on ester bonds carboxylic ester hydrolase activity hydrolase activity catalytic activity phospholipase activity lipase activity cation binding ion binding binding metal ion binding small molecule binding	organic anion transport carboxylic acid transport secretion transport arachidonate transport lipid localization lipid transport establishment of localization organic acid transport localization arachidonate secretion monocarboxylic acid transport fatty acid transport icosanoid transport macromolecule localization organic anion transport carboxylic acid transport secretion transport arachidonate transport lipid localization lipid transport establishment of localization organic acid transport localization arachidonate secretion monocarboxylic acid transport fatty acid transport icosanoid transport macromolecule localization icosanoid secretion long-chain fatty acid transport phospholipid metabolic process organophosphate metabolic process phosphate-containing compound metabolic process metabolic process cellular process primary metabolic process phosphorus metabolic process lipid metabolic process	-

InterPro: Protein Family Classification InterPro Database Homepage

Chains	Accession	Name	Type
A	IPR036444	Phospholipase A2 domain superfamily	Homologous Superfamily
A	IPR015141	Phospholipase A2, prokaryotic/fungal	Family

Membrane Protein Annotation: OPM OPM Database Homepage

Chains	External Link	Type	Class	Superfamily	Family
A	OPM	Monotopic/peripheral	All alpha monotopic/peripheral	Secretory phospholipase A2	Prokaryotic and fungi phospholipase A2

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.