3cwo

X-ray diffraction
3.1Å resolution

A beta/alpha-barrel built by the combination of fragments from different folds

Released:
Source organism: Thermotoga maritima
Primary publication:
A beta alpha-barrel built by the combination of fragments from different folds.
Proc Natl Acad Sci U S A 105 9942-7 (2008)
PMID: 18632584

Function and Biology Details

Reaction catalysed:
(1a) L-glutamine + H(2)O = L-glutamate + NH(3)
Biochemical function:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assemblies composition:
homo dimer
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-194692 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Imidazole glycerol phosphate synthase subunit HisF Chain: X
Molecule details ›
Chain: X
Length: 237 amino acids
Theoretical weight: 26.05 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9X0C6 (Residues: 28-253; Coverage: 88%)
Gene names: TM_1036, hisF
Sequence domains: Histidine biosynthesis protein
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X10SA
Spacegroup: P41212
Unit cell:
a: 108.84Å b: 108.84Å c: 80.41Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.222 0.221 0.256
Expression system: Escherichia coli