› 1ka9

X-ray diffraction
2.3Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181947 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Imidazole glycerol phosphate synthase subunit HisH Chain: H
Molecule details ›
Chain: H
Length: 200 amino acids
Theoretical weight: 21.85 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7SIC0 (Residues: 1-200; Coverage: 100%)
Gene names: TTHA0430, hisH
Sequence domains:
Structure domains: Rossmann fold
Imidazole glycerol phosphate synthase subunit HisF Chain: F
Molecule details ›
Chain: F
Length: 252 amino acids
Theoretical weight: 26.99 KDa
Source organism: Thermus thermophilus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7SIB9 (Residues: 1-252; Coverage: 100%)
Gene names: TTHA1444, hisF
Sequence domains: Histidine biosynthesis protein
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P43212
Unit cell:
a: 82.259Å b: 82.259Å c: 156.183Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.256
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

7 mentions without citation

Architectures and functional coverage of protein-protein interfaces.
Tuncbag et al. (2008)
6 more