› 1w3n

X-ray diffraction
2.1Å resolution

Sulfolobus solfataricus 2-keto-3-deoxygluconate (KDG) aldolase complex with D-KDG

Released:
DOI: 10.2210/pdb1w3n/pdb
PDB entry 1w3n coloured by chain, front view.
PDB entry 1w3n coloured by chain, side view.
PDB entry 1w3n coloured by chain, top view.
Source organism: Saccharolobus solfataricus
Primary publication:
The structural basis for substrate promiscuity in 2-keto-3-deoxygluconate aldolase from the Entner-Doudoroff pathway in Sulfolobus solfataricus.
Theodossis A, Walden H, Westwick EJ, Connaris H, Lamble HJ, Hough DW, Danson MJ, Taylor GL
J Biol Chem 279 43886-92 (2004)
PMID: 15265860

Function and Biology Details

Reaction catalysed: 
2-dehydro-3-deoxy-6-phospho-D-galactonate = pyruvate + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129490 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-dehydro-3-deoxy-phosphogluconate/2-dehydro-3-deoxy-6-phosphogalactonate aldolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 294 amino acids
Theoretical weight: 33.15 KDa
Source organism: Saccharolobus solfataricus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O54288 (Residues: 1-294; Coverage: 100%)
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand SSH 4 x SSH
Ligand GOL 3 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P212121
Unit cell:
a: 83.797Å b: 131.269Å c: 132.759Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.151 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

11 review citations

Enzyme promiscuity: a mechanistic and evolutionary perspective.
Khersonsky et al. (2010)
10 more

5 mentions without citation

Rational approaches for engineering novel functionalities in carbon-carbon bond forming enzymes.
Baker et al. (2012)
4 more