› 4eac

X-ray diffraction
2.3Å resolution

Crystal structure of mannonate dehydratase from Escherichia coli strain K12

Released:
DOI: 10.2210/pdb4eac/pdb
PDB entry 4eac coloured by chain, front view.
PDB entry 4eac coloured by chain, side view.
PDB entry 4eac coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structural insights into decreased enzymatic activity induced by an insert sequence in mannonate dehydratase from Gram negative bacterium.
Qiu X, Tao Y, Zhu Y, Yuan Y, Zhang Y, Liu H, Gao Y, Teng M, Niu L
J Struct Biol 180 327-34 (2012)
PMID: 22796868

Function and Biology Details

Reaction catalysed: 
D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-150174 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mannonate dehydratase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 414 amino acids
Theoretical weight: 47.07 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P24215 (Residues: 1-394; Coverage: 100%)
Gene names: JW4285, b4322, uxuA
Sequence domains: D-mannonate dehydratase (UxuA)
Structure domains: Divalent-metal-dependent TIM barrel enzymes

Ligands and Environments

2 bound ligands:
Ligand CL 4 x CL
Ligand MN 4 x MN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21212
Unit cell:
a: 158.961Å b: 238.461Å c: 54.345Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.183 0.219
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structure and function of aldopentose catabolism enzymes involved in oxidative non-phosphorylative pathways.
Ren et al. (2022)
2 other articles