3Q4Y

Crystal structure of group I phospholipase A2 at 2.3 A resolution in 40% ethanol revealed the critical elements of hydrophobicity of the substrate-binding site

Functional Information from GO Data

Chain	GOid	namespace	contents
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	0006633	biological_process	fatty acid biosynthetic process
A	0006644	biological_process	phospholipid metabolic process
A	0016042	biological_process	lipid catabolic process
A	0016787	molecular_function	hydrolase activity
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

Functional Information from PDB Data

site_id	AC1
Number of Residues	4
Details	BINDING SITE FOR RESIDUE CA A 121

Chain	Residue
A	TYR28
A	GLY30
A	GLY32
A	ASP49

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site_id	AC2
Number of Residues	3
Details	BINDING SITE FOR RESIDUE EOH A 122

Chain	Residue
A	PHE5
A	TRP19
A	ALA23

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Functional Information from PROSITE/UniProt

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

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. VCDCDRLAaIC

Chain	Residue	Details
A	VAL90-CYS100

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:15823962

Chain	Residue	Details
A	HIS48
A	ASP94

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:15823962, ECO:0007744|PDB:1OXR

Chain	Residue	Details
A	TYR28
A	GLY30
A	GLY32
A	ASP49

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