2OOF

The crystal structure of 4-imidazolone-5-propanoate amidohydrolase from environmental sample

Functional Information from GO Data

Chain	GOid	namespace	contents
A	0005506	molecular_function	iron ion binding
A	0005737	cellular_component	cytoplasm
A	0006547	biological_process	L-histidine metabolic process
A	0006548	biological_process	L-histidine catabolic process
A	0008270	molecular_function	zinc ion binding
A	0016787	molecular_function	hydrolase activity
A	0016810	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
A	0016812	molecular_function	hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
A	0019556	biological_process	L-histidine catabolic process to glutamate and formamide
A	0019557	biological_process	L-histidine catabolic process to glutamate and formate
A	0046872	molecular_function	metal ion binding
A	0050480	molecular_function	imidazolonepropionase activity

Functional Information from PDB Data

site_id	AC1
Number of Residues	5
Details	BINDING SITE FOR RESIDUE FE A 500

Chain	Residue
A	HIS72
A	HIS74
A	HIS242
A	ASP317
A	HOH701

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Functional Information from SwissProt/UniProt

site_id	SWS_FT_FI1
Number of Residues	7
Details	Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_00372","evidenceCode":"ECO:0000255"}]}

Chain

Residue

Details

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site_id	SWS_FT_FI2
Number of Residues	4
Details	Binding site: {"evidences":[{"source":"PubMed","id":"18442260","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"2Q09","evidenceCode":"ECO:0007744"}]}

Chain

Residue

Details

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