1UMV

Crystal structure of an acidic, non-myotoxic phospholipase A2 from the venom of Bothrops jararacussu

Functional Information from GO Data

Chain	GOid	namespace	contents
X	0004623	molecular_function	phospholipase A2 activity
X	0005509	molecular_function	calcium ion binding
X	0005543	molecular_function	phospholipid binding
X	0005576	cellular_component	extracellular region
X	0006644	biological_process	phospholipid metabolic process
X	0008217	biological_process	regulation of blood pressure
X	0016042	biological_process	lipid catabolic process
X	0016787	molecular_function	hydrolase activity
X	0035821	biological_process	modulation of process of another organism
X	0042130	biological_process	negative regulation of T cell proliferation
X	0042742	biological_process	defense response to bacterium
X	0046872	molecular_function	metal ion binding
X	0047498	molecular_function	calcium-dependent phospholipase A2 activity
X	0050482	biological_process	arachidonic acid secretion
X	0090729	molecular_function	toxin activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA X1123

Chain	Residue
X	TYR27
X	GLY29
X	LEU30
X	GLY31
X	GLY32
X	ASP48

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Functional Information from PROSITE/UniProt

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

Chain	Residue	Details
X	CYS43-CYS50

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

Chain	Residue	Details
X	ILE85-CYS95

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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:16376474

Chain	Residue	Details
X	HIS47
X	ASP89

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site_id	SWS_FT_FI2
Number of Residues	4
Details	BINDING: BINDING => ECO:0000269|PubMed:15351695, ECO:0000269|PubMed:16376474, ECO:0007744|PDB:1UMV, ECO:0007744|PDB:1ZL7

Chain	Residue	Details
X	TYR27
X	GLY32
X	ASP48
X	GLY31

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