› 1ox5

X-ray diffraction
2.5Å resolution

TOWARDS UNDERSTANDING THE MECHANISM OF THE COMPLEX CYCLIZATION REACTION CATALYZED BY IMIDAZOLE GLYCEROPHOSPHATE SYNTHASE

Released:
DOI: 10.2210/pdb1ox5/pdb
PDB entry 1ox5 coloured by chain, front view.
PDB entry 1ox5 coloured by chain, side view.
PDB entry 1ox5 coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Toward understanding the mechanism of the complex cyclization reaction catalyzed by imidazole glycerolphosphate synthase: crystal structures of a ternary complex and the free enzyme.
Chaudhuri BN, Lange SC, Myers RS, Davisson VJ, Smith JL
Biochemistry 42 7003-12 (2003)
PMID: 12795595

Function and Biology Details

Reactions catalysed: 
L-glutamine + H(2)O = L-glutamate + NH(3)
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152640 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Imidazole glycerol phosphate synthase hisHF Chains: A, B
Molecule details ›
Chains: A, B
Length: 555 amino acids
Theoretical weight: 61.57 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P33734 (Residues: 1-552; Coverage: 100%)
Gene names: HIS7, YBR1640, YBR248C
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand NI 1 x NI
Ligand 1PR 2 x 1PR
1 modified residue:
Ligand 5CS 2 x 5CS

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 98.8Å b: 111.5Å c: 117.2Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.223 0.246
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Gates of enzymes.
Gora et al. (2013)
4 more

14 mentions without citation

NMR Methods to Study Dynamic Allostery.
Grutsch et al. (2016)
13 more