› 1jvn

X-ray diffraction
2.1Å resolution

CRYSTAL STRUCTURE OF IMIDAZOLE GLYCEROL PHOSPHATE SYNTHASE: A TUNNEL THROUGH A (BETA/ALPHA)8 BARREL JOINS TWO ACTIVE SITES

Released:
DOI: 10.2210/pdb1jvn/pdb
PDB entry 1jvn coloured by chain, front view.
PDB entry 1jvn coloured by chain, side view.
PDB entry 1jvn coloured by chain, top view.
Source organism: Saccharomyces cerevisiae
Primary publication:
Crystal structure of imidazole glycerol phosphate synthase: a tunnel through a (beta/alpha)8 barrel joins two active sites.
Chaudhuri BN, Lange SC, Myers RS, Chittur SV, Davisson VJ, Smith JL
Structure 9 987-97 (2001)
PMID: 11591353

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: 61.56 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P33734 (Residues: 1-552; Coverage: 100%)
Gene names: HIS7, YBR1640, YBR248C
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand NI 2 x NI
Ligand SO4 5 x SO4
Ligand POP 1 x POP
1 modified residue:
Ligand 143 2 x 143

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 17-ID, APS BEAMLINE 14-BM-D
Spacegroup: P212121
Unit cell:
a: 98.37Å b: 112.173Å c: 116.68Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.224 0.242
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

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

11 mentions without citation

Tunnel Architectures in Enzyme Systems that Transport Gaseous Substrates.
Singh et al. (2021)
10 more