› 1vhc

X-ray diffraction
1.89Å resolution

Function and Biology Details

Reactions catalysed: 
2-dehydro-3-deoxy-6-phosphate-D-gluconate = pyruvate + D-glyceraldehyde 3-phosphate
(4R)-4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-155178 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative KHG/KDPG aldolase Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 224 amino acids
Theoretical weight: 24.48 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
  • Canonical: P44480 (Residues: 2-212; Coverage: 100%)
Gene names: HI_0047, eda
Sequence domains: KDPG and KHG aldolase
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 30 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 32-ID
Spacegroup: P21
Unit cell:
a: 77.271Å b: 133.227Å c: 89.733Å
α: 90° β: 105.82° γ: 90°
R-values:
R R work R free
0.219 0.219 0.256
Expression system: Escherichia coli

Quick links

Citations

23 review citations

Regulation of fatty acid metabolism in bacteria.
Fujita et al. (2007)
22 more

2 mentions without citation

A fragment-based protein interface design algorithm for symmetric assemblies.
Laniado et al. (2021)
1 more