Structure of PDB 2oof Chain A

Receptor sequence

>2oofA (length=403) Species: 32644 (unidentified)

LNCERVWLNVTPATLRSDLADYGLLEPHALGVHEGRIHALVPMQDLKYPA
HWQDMKGKLVTPGLIDCHTHLIFAGSRAEEFELRQKGVPYAEIARKGGGI
ISTVRATRAASEDQLFELALPRVKSLIREGVTTVEIKSGYGLTLEDELKM
LRVARRLGEALPIRVKTTLLAAHAVPPEYRDDPDSWVETICQEIIPAAAE
AGLADAVDVFCEHIGFSLAQTEQVYLAADQYGLAVKGHMDQLSNLGGSTL
AANFGALSVDHLEYLDPEGIQALAHRGVVATLLPTAFYFLKETKLPPVVA
LRKAGVPMAVSSDINPGTAPIVSLRMAMNMACTLFGLTPVEAMAGVTRHA
ARALGEQEQLGQLRVGMLADFLVWNCGHPAELSYLIGVDQLVSRVVNGEE
TLH

3D structure

• PDB: 2oof The crystal structure of 4-imidazolone-5-propanoate amidohydrolase from environmental sample
• Chain: A
• Resolution: 2.2 Å

Enzymatic activity

• Enzyme Commision number: 3.5.2.7: imidazolonepropionase.

Interaction with ligand

Site #	Ligand	Ligand chain	Binding residues on receptor (original residue number in PDB)	Binding residues on receptor (residue number reindexed from 1)	Binding affinity
BS01	FE	A	H72 H74 H242 D317	H68 H70 H238 D313

Gene Ontology

Molecular Function

• GO:0005506 iron ion binding
• GO:0008270 zinc ion binding
• GO:0016787 hydrolase activity
• GO:0016810 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds
• GO:0016812 hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides
• GO:0046872 metal ion binding
• GO:0050480 imidazolonepropionase activity

Biological Process

• GO:0006547 L-histidine metabolic process
• GO:0006548 L-histidine catabolic process
• GO:0019556 L-histidine catabolic process to glutamate and formamide
• GO:0019557 L-histidine catabolic process to glutamate and formate

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:2oof, PDBe:2oof, PDBj:2oof
• PDBsum: 2oof
• UniProt: A0KF84|HUTI_AERHH Imidazolonepropionase (Gene Name=hutI)