› 2q1c

X-ray diffraction
2.8Å resolution

2-keto-3-deoxy-D-arabinonate dehydratase complexed with calcium and 2-oxobutyrate

Released:
DOI: 10.2210/pdb2q1c/pdb
Model geometry
Fit model/data
PDB entry 2q1c coloured by chain, front view.
PDB entry 2q1c coloured by chain, side view.
PDB entry 2q1c coloured by chain, top view.
Source organism: Saccharolobus solfataricus P2
Primary publication:
Structural insight into substrate binding and catalysis of a novel 2-keto-3-deoxy-D-arabinonate dehydratase illustrates common mechanistic features of the FAH superfamily.
Brouns SJ, Barends TR, Worm P, Akerboom J, Turnbull AP, Salmon L, van der Oost J
J Mol Biol 379 357-71 (2008)
PMID: 18448118

Function and Biology Details

Reaction catalysed: 
2-dehydro-3-deoxy-D-arabinonate = 2,5-dioxopentanoate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-188976 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
2-dehydro-3-deoxy-D-arabinonate dehydratase Chain: X
Molecule details ›
Chain: X
Length: 293 amino acids
Theoretical weight: 33.19 KDa
Source organism: Saccharolobus solfataricus P2
Expression system: Escherichia coli
UniProt:
  • Canonical: Q97UA0 (Residues: 6-298; Coverage: 98%)
Gene names: SSO3118, kdaD
Sequence domains: Fumarylacetoacetate (FAA) hydrolase C-terminal
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand 2KT 1 x 2KT
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: I4122
Unit cell:
a: 129.29Å b: 129.29Å c: 223.09Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.241 0.24 0.266
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.
Bräsen et al. (2014)
3 more

1 mention without citation

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