1YXH

Crystal structure of a novel phospholipase A2 from Naja naja sagittifera with a strong anticoagulant activity

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0004623	molecular_function	phospholipase A2 activity
A	0005509	molecular_function	calcium ion binding
A	0006644	biological_process	phospholipid metabolic process
A	0016042	biological_process	lipid catabolic process
A	0050482	biological_process	arachidonate secretion

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE CA A 1001

Chain	Residue
A	TYR28
A	GLY30
A	GLY32
A	ASP49
A	EOH2002
A	HOH3050

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site_id	AC2
Number of Residues	2
Details	BINDING SITE FOR RESIDUE PO4 A 3001

Chain	Residue
A	SER34
A	GLN120

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site_id	AC3
Number of Residues	2
Details	BINDING SITE FOR RESIDUE EOH A 2001

Chain	Residue
A	EOH2002
A	PHE22

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site_id	AC4
Number of Residues	6
Details	BINDING SITE FOR RESIDUE EOH A 2002

Chain	Residue
A	TYR28
A	GLY30
A	ASP49
A	CA1001
A	EOH2001
A	HOH3052

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Functional Information from PROSITE/UniProt

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

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	Active site: {"evidences":[{"source":"PubMed","id":"16269164","evidenceCode":"ECO:0000305"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"16269164","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1YXH","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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