3I3I

Crystal Structure of Bothropstoxin-I crystallized at 283 K

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	0008201	molecular_function	heparin binding
A	0016042	biological_process	lipid catabolic process
A	0035821	biological_process	modulation of process of another organism
A	0042130	biological_process	negative regulation of T cell proliferation
A	0042742	biological_process	defense response to bacterium
A	0047498	molecular_function	calcium-dependent phospholipase A2 activity
A	0050482	biological_process	arachidonic acid secretion
A	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. CCYvHKcC

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. LCECDKAVaIC

Chain	Residue	Details
A	LEU95-CYS105

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	SITE: Important residue of the cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6

Chain	Residue	Details
A	LYS115
A	ARG118

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site_id	SWS_FT_FI2
Number of Residues	2
Details	SITE: Hydrophobic membrane-disruption site (MDiS) => ECO:0000250|UniProtKB:I6L8L6

Chain	Residue	Details
A	LEU121
A	PHE125

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site_id	SWS_FT_FI3
Number of Residues	2
Details	SITE: Cationic membrane-docking site (MDoS) => ECO:0000250|UniProtKB:I6L8L6

Chain	Residue	Details
A	LYS122
A	LYS129

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