3IVZ

Crystal structure of hyperthermophilic nitrilase

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0000257	molecular_function	nitrilase activity
A	0003837	molecular_function	beta-ureidopropionase activity
A	0006807	biological_process	obsolete nitrogen compound metabolic process
A	0016787	molecular_function	hydrolase activity
A	0033388	biological_process	putrescine biosynthetic process from arginine
A	0033396	biological_process	beta-alanine biosynthetic process via 3-ureidopropionate
A	0050126	molecular_function	N-carbamoylputrescine amidase activity
A	0080061	molecular_function	indole-3-acetonitrile nitrilase activity
B	0000257	molecular_function	nitrilase activity
B	0003837	molecular_function	beta-ureidopropionase activity
B	0006807	biological_process	obsolete nitrogen compound metabolic process
B	0016787	molecular_function	hydrolase activity
B	0033388	biological_process	putrescine biosynthetic process from arginine
B	0033396	biological_process	beta-alanine biosynthetic process via 3-ureidopropionate
B	0050126	molecular_function	N-carbamoylputrescine amidase activity
B	0080061	molecular_function	indole-3-acetonitrile nitrilase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	6
Details	BINDING SITE FOR RESIDUE MG A 263

Chain	Residue
A	MET222
A	HOH285
A	HOH294
A	HOH314
A	HOH321
A	HOH323

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	2
Details	ACT_SITE: Proton acceptor => ECO:0000305|PubMed:21095228

Chain	Residue	Details
A	GLU42
B	GLU42

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site_id	SWS_FT_FI2
Number of Residues	2
Details	ACT_SITE: Proton donor => ECO:0000305|PubMed:21095228

Chain	Residue	Details
A	LYS113
B	LYS113

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site_id	SWS_FT_FI3
Number of Residues	2
Details	ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00054, ECO:0000269|PubMed:21095228

Chain	Residue	Details
A	CSX146
B	CSX146

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site_id	SWS_FT_FI4
Number of Residues	2
Details	BINDING: BINDING => ECO:0000255

Chain	Residue	Details
A	VAL173
B	VAL173

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