1POC

CRYSTAL STRUCTURE OF BEE-VENOM PHOSPHOLIPASE A2 IN A COMPLEX WITH A TRANSITION-STATE ANALOGUE

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004623	molecular_function	phospholipase A2 activity
A	0005509	molecular_function	calcium ion binding
A	0005576	cellular_component	extracellular region
A	0006629	biological_process	lipid metabolic 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	0050482	biological_process	arachidonate secretion

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE CA A 501

Chain	Residue
A	TRP8
A	GLY10
A	GLY12
A	ASP35
A	GEL420

---

site_id	AC2
Number of Residues	13
Details	BINDING SITE FOR RESIDUE GEL A 420

Chain	Residue
A	ILE1
A	TRP8
A	GLY10
A	HIS11
A	GLY12
A	HIS34
A	ASP35
A	THR57
A	PHE67
A	PHE82
A	MET86
A	TYR87
A	CA501

---

site_id	CA1
Number of Residues	4
Details

Chain	Residue
A	TRP8
A	GLY10
A	GLY12
A	ASP35

---

Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
A	CYS30-CYS37

---

Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	Active site: {"evidences":[{"source":"PubMed","id":"2274788","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"2274788","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1POC","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

---

site_id	SWS_FT_FI3
Number of Residues	1
Details	Glycosylation: {"description":"N-linked (GlcNAc...) asparagine","featureId":"CAR_000001","evidences":[{"source":"PubMed","id":"8504812","evidenceCode":"ECO:0000269"}]}

Chain

Residue

Details

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