1P2P

STRUCTURE OF PORCINE PANCREATIC PHOSPHOLIPASE A2 AT 2.6 ANGSTROMS RESOLUTION AND COMPARISON WITH BOVINE PHOSPHOLIPASE A2

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0002446	biological_process	neutrophil mediated immunity
A	0004623	molecular_function	phospholipase A2 activity
A	0005102	molecular_function	signaling receptor binding
A	0005509	molecular_function	calcium ion binding
A	0005543	molecular_function	phospholipid binding
A	0005576	cellular_component	extracellular region
A	0006629	biological_process	lipid metabolic process
A	0006633	biological_process	fatty acid biosynthetic process
A	0006644	biological_process	phospholipid metabolic process
A	0008284	biological_process	positive regulation of cell population proliferation
A	0009986	cellular_component	cell surface
A	0010524	biological_process	positive regulation of calcium ion transport into cytosol
A	0016042	biological_process	lipid catabolic process
A	0016787	molecular_function	hydrolase activity
A	0019370	biological_process	leukotriene biosynthetic process
A	0030593	biological_process	neutrophil chemotaxis
A	0032052	molecular_function	bile acid binding
A	0032652	biological_process	regulation of interleukin-1 production
A	0032757	biological_process	positive regulation of interleukin-8 production
A	0032869	biological_process	cellular response to insulin stimulus
A	0035556	biological_process	intracellular signal transduction
A	0043406	biological_process	positive regulation of MAP kinase activity
A	0045944	biological_process	positive regulation of transcription by RNA polymerase II
A	0046324	biological_process	regulation of D-glucose import
A	0046470	biological_process	phosphatidylcholine metabolic process
A	0046471	biological_process	phosphatidylglycerol metabolic process
A	0046872	molecular_function	metal ion binding
A	0047498	molecular_function	calcium-dependent phospholipase A2 activity
A	0047499	molecular_function	calcium-independent phospholipase A2 activity
A	0048146	biological_process	positive regulation of fibroblast proliferation
A	0050482	biological_process	arachidonate secretion
A	0050778	biological_process	positive regulation of immune response
A	0051092	biological_process	positive regulation of NF-kappaB transcription factor activity
A	1904635	biological_process	positive regulation of podocyte apoptotic process

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 125

Chain	Residue
A	TYR28
A	GLY30
A	GLY32
A	ASP49

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site_id	AC2
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 126

Chain	Residue
A	SER72
A	SER72
A	GLU92
A	GLU92

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Functional Information from PROSITE/UniProt

site_id	PS00118
Number of Residues	8
Details	PA2_HIS Phospholipase A2 histidine active site. CCEtHDnC

Chain	Residue	Details
A	CYS44-CYS51

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site_id	PS00119
Number of Residues	11
Details	PA2_ASP Phospholipase A2 aspartic acid active site. ICNCDRNAaIC

Chain	Residue	Details
A	ILE95-CYS105

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000269|PubMed:6876174

Chain	Residue	Details
A	HIS48
A	ASP99

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P00593

Chain	Residue	Details
A	TYR28
A	GLY30
A	GLY32
A	ASP49

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site_id	SWS_FT_FI3
Number of Residues	1
Details	LIPID: N6-palmitoyl lysine => ECO:0000269|PubMed:2498336

Chain	Residue	Details
A	LYS56

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
A	HIS48
A	GLY30
A	ASP99

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site_id	MCSA1
Number of Residues	8
Details	M-CSA 83

Chain	Residue	Details
A	TYR28	metal ligand
A	GLY30	metal ligand
A	GLY32	metal ligand
A	HIS48	electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor
A	ASP49	metal ligand
A	TYR52	electrostatic stabiliser, hydrogen bond donor
A	TYR73	electrostatic stabiliser, hydrogen bond donor
A	ASP99	electrostatic stabiliser, hydrogen bond acceptor

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