X-ray diffraction
1.7Å resolution

Crystal structure of the mutant P317A of d-mannonate dehydratase from chromohalobacter salexigens complexed with mg and d-gluconate

Entry authors: Fedorov AA, Fedorov EV, Wichelecki D, Gerlt JA, Almo SC

Function and Biology Details

Reactions catalysed:
D-mannonate = 2-dehydro-3-deoxy-D-gluconate + H(2)O
D-gluconate = 2-dehydro-3-deoxy-D-gluconate + H(2)O
Biochemical function:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
D-galactonate dehydratase family member ManD Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 405 amino acids
Theoretical weight: 45.44 KDa
Source organism: Chromohalobacter salexigens DSM 3043
Expression system: Escherichia coli
  • Canonical: Q1QT89 (Residues: 2-403; Coverage: 100%)
Gene names: Csal_2974, manD
Sequence domains:
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 196.334Å b: 85.79Å c: 195.638Å
α: 90° β: 110.47° γ: 90°
R R work R free
0.17 0.169 0.203
Expression system: Escherichia coli