Structure of PDB 2g3f Chain B

Receptor sequence

>2g3fB (length=414) Species: 1423 (Bacillus subtilis)

PKQIDTILINIGQLLTMESSGPRAGKSMQDLHVIEDAVVGIHEQKIVFAG
QKGAEAGYEADEIIDCSGRLVTPGLVDPHTHLVFGGSREKEMNLKLQGIS
YLDILAQGGGILSTVKDTRAASEEELLQKAHFHLQRMLSYGTTTAEVKSG
YGLEKETELKQLRVAKKLHESQPVDLVSTFMGAHAIPPEYQNDPDDFLDQ
MLSLLPEIKEQELASFADIFTETGVFTVSQSRRYLQKAAEAGFGLKIHAD
EIDPLGGAELAGKLKAVSADHLVGTSDEGIKKLAEAGTIAVLLPGTTFYL
GKSTYARARAMIDEGVCVSLATDFNPGSSPTENIQLIMSIAALHLKMTAE
EIWHAVTVNAAYAIGKGEEAGQLKAGRSADLVIWQAPNYMYIPYHYGVNH
VHQVMKNGTIVVNR

3D structure

• PDB: 2g3f A catalytic mechanism revealed by the crystal structures of the imidazolonepropionase from Bacillus subtilis
• Chain: B
• Resolution: 2.0 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	ZN	B	H80 H82 H249 D324	H79 H81 H248 D323
BS02	IZC	B	R89 Y102 I112 Y152 F221 E252 N326 S329	R88 Y101 I111 Y151 F220 E251 N325 S328

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:2g3f, PDBe:2g3f, PDBj:2g3f
• PDBsum: 2g3f
• PubMed: 16990261
• UniProt: P42084|HUTI_BACSU Imidazolonepropionase (Gene Name=hutI)