1wau

X-ray diffraction
2.8Å resolution

Structure of KDPG Aldolase E45N mutant

Released:
Source organism: Escherichia coli

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
Biological process:
  • not assigned
Cellular component:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141815 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
KHG/KDPG aldolase Chain: A
Molecule details ›
Chain: A
Length: 213 amino acids
Theoretical weight: 22.29 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0A955 (Residues: 1-213; Coverage: 100%)
Gene names: JW1839, b1850, eda, hga, kdgA
Sequence domains: KDPG and KHG aldolase
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P321
Unit cell:
a: 105.195Å b: 105.195Å c: 51.444Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.174 0.171 0.246
Expression system: Escherichia coli BL21(DE3)