Structure of PDB 2gok Chain B

Receptor sequence

>2gokB (length=404) Species: 176299 (Agrobacterium fabrum str. C58)

ATALWRNAQLATLNPAMDGIGAVENAVIAVRNGRIAFAGPESDLPDDLST
ADETTDCGGRWITPALIDCHTHLVFGGNRAMEFEMRLNGATYEEIAKAGG
GIVSSVRDTRALSDEVLVAQALPRLDTLLSEGVSTIEIKSGYGLDIETEL
KMLRVARRLETLRPVRIVTSYLAAHATPADYKGRNADYITDVVLPGLEKA
HAEGLADAVDGFCEGIAFSVKEIDRVFAAAQQRGLPVKLHAEQLSNLGGA
ELAASYNALSADHLEYLDETGAKALAKAGTVAVLLPGAFYALREKQLPPV
QALRDAGAEIALATDCNPGTSPLTSLLLTMNMGATLFRMTVEECLTATTR
NAAKALGLLAETGTLEAGKSADFAIWDIERPAELVYRIGFNPLHARIFKG
QKVS

3D structure

• PDB: 2gok X-ray structure of imidazolonepropionase from Agrobacterium tumefaciens at 1.87 A resolution.
• Chain: B
• Resolution: 1.87 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	B	H86 H88 H256 D331	H70 H72 H240 D315

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:2gok, PDBe:2gok, PDBj:2gok
• PDBsum: 2gok
• PubMed: 17640072
• UniProt: Q8U8Z6|HUTI_AGRFC Imidazolonepropionase (Gene Name=hutI)