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Phospholipase A2 from Vipera ammodytes meridionalis

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004623	molecular_function	phospholipase A2 activity
A	0005509	molecular_function	calcium ion binding
A	0005543	molecular_function	phospholipid binding
A	0005576	cellular_component	extracellular region
A	0006644	biological_process	phospholipid metabolic process
A	0016042	biological_process	lipid catabolic process
A	0016787	molecular_function	hydrolase activity
A	0031640	biological_process	killing of cells of another organism
A	0035821	biological_process	modulation of process of another organism
A	0042130	biological_process	negative regulation of T cell proliferation
A	0046872	molecular_function	metal ion binding
A	0047498	molecular_function	calcium-dependent phospholipase A2 activity
A	0050482	biological_process	arachidonic acid secretion
A	0090729	molecular_function	toxin activity
B	0004623	molecular_function	phospholipase A2 activity
B	0005509	molecular_function	calcium ion binding
B	0005543	molecular_function	phospholipid binding
B	0005576	cellular_component	extracellular region
B	0006644	biological_process	phospholipid metabolic process
B	0016042	biological_process	lipid catabolic process
B	0016787	molecular_function	hydrolase activity
B	0031640	biological_process	killing of cells of another organism
B	0035821	biological_process	modulation of process of another organism
B	0042130	biological_process	negative regulation of T cell proliferation
B	0046872	molecular_function	metal ion binding
B	0047498	molecular_function	calcium-dependent phospholipase A2 activity
B	0050482	biological_process	arachidonic acid secretion
B	0090729	molecular_function	toxin activity
K	0004623	molecular_function	phospholipase A2 activity
K	0005509	molecular_function	calcium ion binding
K	0005543	molecular_function	phospholipid binding
K	0005576	cellular_component	extracellular region
K	0006644	biological_process	phospholipid metabolic process
K	0016042	biological_process	lipid catabolic process
K	0016787	molecular_function	hydrolase activity
K	0031640	biological_process	killing of cells of another organism
K	0035821	biological_process	modulation of process of another organism
K	0042130	biological_process	negative regulation of T cell proliferation
K	0046872	molecular_function	metal ion binding
K	0047498	molecular_function	calcium-dependent phospholipase A2 activity
K	0050482	biological_process	arachidonic acid secretion
K	0090729	molecular_function	toxin activity
L	0004623	molecular_function	phospholipase A2 activity
L	0005509	molecular_function	calcium ion binding
L	0005543	molecular_function	phospholipid binding
L	0005576	cellular_component	extracellular region
L	0006644	biological_process	phospholipid metabolic process
L	0016042	biological_process	lipid catabolic process
L	0016787	molecular_function	hydrolase activity
L	0031640	biological_process	killing of cells of another organism
L	0035821	biological_process	modulation of process of another organism
L	0042130	biological_process	negative regulation of T cell proliferation
L	0046872	molecular_function	metal ion binding
L	0047498	molecular_function	calcium-dependent phospholipase A2 activity
L	0050482	biological_process	arachidonic acid secretion
L	0090729	molecular_function	toxin activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	15
Details	BINDING SITE FOR RESIDUE ELD B 134

Chain	Residue
A	GLY30
B	CYS45
B	HIS48
B	ASP49
B	LYS69
B	ALA102
B	PHE106
A	TRP31
A	CYS45
A	HIS48
A	ASP49
B	LEU2
B	PHE5
B	TRP31
B	CYS44

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site_id	AC2
Number of Residues	17
Details	BINDING SITE FOR RESIDUE ELD L 134

Chain	Residue
K	LEU2
K	TYR28
K	CYS29
K	GLY30
K	TRP31
K	CYS45
K	HIS48
K	LYS69
L	LEU2
L	PHE5
L	TYR22
L	GLY30
L	TRP31
L	CYS44
L	CYS45
L	ALA102
L	PHE106

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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
A	CYS44-CYS51

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

Chain	Residue	Details
A	ILE95-CYS105

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	8
Details	ACT_SITE: ACT_SITE => ECO:0000305|PubMed:9276469

Chain	Residue	Details
A	HIS48
A	ASP99
B	HIS48
B	ASP99
K	HIS48
K	ASP99
L	HIS48
L	ASP99

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site_id	SWS_FT_FI2
Number of Residues	16
Details	BINDING: BINDING => ECO:0000250|UniProtKB:P14418

Chain	Residue	Details
A	TYR28
K	GLY30
K	GLY32
K	ASP49
L	TYR28
L	GLY30
L	GLY32
L	ASP49
A	GLY30
A	GLY32
A	ASP49
B	TYR28
B	GLY30
B	GLY32
B	ASP49
K	TYR28

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