5TFV

Crystal Structure of MT-I isolated from Bothrops asper venom.

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	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	0046872	molecular_function	metal ion binding
A	0047498	molecular_function	calcium-dependent phospholipase A2 activity
A	0047499	molecular_function	calcium-independent 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	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	0042130	biological_process	negative regulation of T cell proliferation
B	0042742	biological_process	defense response to bacterium
B	0046872	molecular_function	metal ion binding
B	0047498	molecular_function	calcium-dependent phospholipase A2 activity
B	0047499	molecular_function	calcium-independent phospholipase A2 activity
B	0050482	biological_process	arachidonate secretion
B	0090729	molecular_function	toxin activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	3
Details	binding site for residue TRS A 201

Chain	Residue
A	ARG16
A	LYS115
B	ARG72

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site_id	AC2
Number of Residues	6
Details	binding site for residue TRS B 201

Chain	Residue
A	ARG72
A	ARG72
B	ARG16
B	ARG16
B	TYR21
B	LYS115

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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. ICECDKAAaVC

Chain	Residue	Details
A	ILE95-CYS105

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	4
Details	ACT_SITE: ACT_SITE => ECO:0000250

Chain	Residue	Details
A	HIS48
A	ASP99
B	HIS48
B	ASP99

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site_id	SWS_FT_FI2
Number of Residues	8
Details	BINDING: BINDING => ECO:0000250

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

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