Structure of PDB 1ox4 Chain B

Receptor sequence

>1ox4B (length=538) Species: 4932 (Saccharomyces cerevisiae)

GSHMPVVHVIDVESGNLQSLTNAIEHLGYEVQLVKSPKDFNISGTSRLIL
PGVGNYGHFVDNLFNRGFEKPIREYIESGKPIMGICVGLQALFAGSVESP
KSTGLNYIDFKLSRFDDSEKPVPEIGWNSCIPSENLFFGLDPYKRYYFVH
SFAAILNSEKKKNLENDGWKIAKAKYGSEEFIAAVNKNNIFATQFHPEKS
GKAGLNVIENFLKQQSPPIPNYSAEEKELLMNDYSNYGLTRRIIACLDVR
TNDQGDLVVTKGDLGKPVQLAQKYYQQGADEVTFLNITSFRDCPLKDTPM
LEVLKQAAKTVFVPLTVGGGIKDIVDVDGTKIPALEVASLYFRSGADKVS
IGTDAVYAAEKYYELGNRGDGTSPIETISKAYGAQAVVISVDPKRVYVNS
QADTKNKVFETEYPGPNGEKYCWYQCTIKGGRESRDLGVWELTRACEALG
AGEILLNCIDKDGSNSGYDLELIEHVKDAVKIPVIASSGAGVPEHFEEAF
LKTRADACLGAGMFHRGEFTVNDVKEYLLEHGLKVRMD

3D structure

• PDB: 1ox4 Towards Understanding the Mechanism of the Complex Cyclization Reaction Catalyzed by Imidazole Glycerophosphate Synthase: Crystal Structures of a Ternary Complex and the Free Enzyme
• Chain: B
• Resolution: 2.5 Å

Enzymatic activity

• Catalytic site (original residue number in PDB): D245 D404
• Catalytic site (residue number reindexed from 1): D248 D392
• Enzyme Commision number: 3.5.1.2: glutaminase.
  4.3.2.10: imidazole glycerol-phosphate synthase.

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	POP	B	G475 S500 A523 G524	G463 S488 A511 G512

Gene Ontology

Molecular Function

• GO:0000107 imidazoleglycerol-phosphate synthase activity
• GO:0004359 glutaminase activity
• GO:0016763 pentosyltransferase activity
• GO:0016787 hydrolase activity
• GO:0016829 lyase activity
• GO:0016833 oxo-acid-lyase activity

Biological Process

• GO:0000105 L-histidine biosynthetic process
• GO:0006541 glutamine metabolic process
• GO:0044281 small molecule metabolic process

Cellular Component

• GO:0005737 cytoplasm

External links

• PDB: RCSB:1ox4, PDBe:1ox4, PDBj:1ox4
• PDBsum: 1ox4
• PubMed: 12795595
• UniProt: P33734|HIS5_YEAST Imidazole glycerol phosphate synthase hisHF (Gene Name=HIS7)