1G2X

Sequence induced trimerization of krait PLA2: crystal structure of the trimeric form of krait PLA2

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	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	0035821	biological_process	modulation of process of another organism
A	0046872	molecular_function	metal ion binding
A	0047498	molecular_function	calcium-dependent phospholipase A2 activity
A	0050482	biological_process	arachidonate 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	0006629	biological_process	lipid metabolic process
B	0006644	biological_process	phospholipid metabolic process
B	0016042	biological_process	lipid catabolic process
B	0016787	molecular_function	hydrolase activity
B	0035821	biological_process	modulation of process of another organism
B	0046872	molecular_function	metal ion binding
B	0047498	molecular_function	calcium-dependent phospholipase A2 activity
B	0050482	biological_process	arachidonate secretion
B	0090729	molecular_function	toxin activity
C	0004623	molecular_function	phospholipase A2 activity
C	0005509	molecular_function	calcium ion binding
C	0005543	molecular_function	phospholipid binding
C	0005576	cellular_component	extracellular region
C	0006629	biological_process	lipid metabolic process
C	0006644	biological_process	phospholipid metabolic process
C	0016042	biological_process	lipid catabolic process
C	0016787	molecular_function	hydrolase activity
C	0035821	biological_process	modulation of process of another organism
C	0046872	molecular_function	metal ion binding
C	0047498	molecular_function	calcium-dependent phospholipase A2 activity
C	0050482	biological_process	arachidonate secretion
C	0090729	molecular_function	toxin activity

Functional Information from PROSITE/UniProt

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

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. LCDCDRTAaIC

Chain	Residue	Details
A	LEU90-CYS100

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	6
Details	Active site: {"evidences":[{"source":"PubMed","id":"11286555","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	12
Details	Binding site: {"evidences":[{"source":"PubMed","id":"11286555","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1FE5","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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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	ASP94

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site_id	CSA2
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
B	HIS48
B	GLY30
B	ASP94

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site_id	CSA3
Number of Residues	3
Details	Annotated By Reference To The Literature 1n29

Chain	Residue	Details
C	HIS48
C	GLY30
C	ASP94

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