1WOH

Crystal Structure of Agmatinase Reveals Structural Conservation and Inhibition Mechanism of the Ureohydrolase Superfamily

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0008783	molecular_function	agmatinase activity
A	0016787	molecular_function	hydrolase activity
A	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
A	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
A	0046872	molecular_function	metal ion binding
B	0008783	molecular_function	agmatinase activity
B	0016787	molecular_function	hydrolase activity
B	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
B	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
B	0046872	molecular_function	metal ion binding
C	0008783	molecular_function	agmatinase activity
C	0016787	molecular_function	hydrolase activity
C	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
C	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
C	0046872	molecular_function	metal ion binding
D	0008783	molecular_function	agmatinase activity
D	0016787	molecular_function	hydrolase activity
D	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
D	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
D	0046872	molecular_function	metal ion binding
E	0008783	molecular_function	agmatinase activity
E	0016787	molecular_function	hydrolase activity
E	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
E	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
E	0046872	molecular_function	metal ion binding
F	0008783	molecular_function	agmatinase activity
F	0016787	molecular_function	hydrolase activity
F	0016813	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines
F	0033389	biological_process	putrescine biosynthetic process from arginine, via agmatine
F	0046872	molecular_function	metal ion binding

Functional Information from PROSITE/UniProt

site_id	PS01053
Number of Residues	22
Details	ARGINASE_1 Arginase family signature. SVDVDgfdPaviPGtsspepdG

Chain	Residue	Details
A	SER227-GLY248

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Catalytic Information from CSA

site_id	CSA1
Number of Residues	2
Details	Annotated By Reference To The Literature 1cev

Chain	Residue	Details
A	GLU274
A	ASP147

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site_id	CSA2
Number of Residues	2
Details	Annotated By Reference To The Literature 1cev

Chain	Residue	Details
B	GLU274
B	ASP147

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site_id	CSA3
Number of Residues	2
Details	Annotated By Reference To The Literature 1cev

Chain	Residue	Details
C	GLU274
C	ASP147

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site_id	CSA4
Number of Residues	2
Details	Annotated By Reference To The Literature 1cev

Chain	Residue	Details
D	GLU274
D	ASP147

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site_id	CSA5
Number of Residues	2
Details	Annotated By Reference To The Literature 1cev

Chain	Residue	Details
E	GLU274
E	ASP147

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site_id	CSA6
Number of Residues	2
Details	Annotated By Reference To The Literature 1cev

Chain	Residue	Details
F	GLU274
F	ASP147

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