› 4ewn

X-ray diffraction
1.9Å resolution

Structure of HisF-D130V+D176V with bound rCdRP

Released:
DOI: 10.2210/pdb4ewn/pdb
PDB entry 4ewn coloured by chain, front view.
PDB entry 4ewn coloured by chain, side view.
PDB entry 4ewn coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
A sugar isomerization reaction established on various (βα)₈-barrel scaffolds is based on substrate-assisted catalysis.
Reisinger B, Bocola M, List F, Claren J, Rajendran C, Sterner R
Protein Eng Des Sel 25 751-60 (2012)
PMID: 23109729

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194692 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Imidazole glycerol phosphate synthase subunit HisF Chain: D
Molecule details ›
Chain: D
Length: 253 amino acids
Theoretical weight: 27.72 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0C6 (Residues: 1-253; Coverage: 100%)
Gene names: TM_1036, hisF
Sequence domains: Histidine biosynthesis protein
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand 0VR 1 x 0VR
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: F222
Unit cell:
a: 57.654Å b: 112.517Å c: 163.402Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.204 0.236
Expression system: Escherichia coli

Quick links

Citations

1 review citation

How enzyme promiscuity and horizontal gene transfer contribute to metabolic innovation.
Glasner et al. (2020)
4 other articles

2 mentions without citation

The Role of Gene Elongation in the Evolution of Histidine Biosynthetic Genes.
Del Duca et al. (2020)
1 more