› 1p1x

X-ray diffraction
0.99Å resolution

Comparison of class I aldolase binding site architecture based on the crystal structure of 2-deoxyribose-5-phosphate aldolase determined at 0.99 Angstrom resolution

Released:
DOI: 10.2210/pdb1p1x/pdb
PDB entry 1p1x coloured by chain, front view.
PDB entry 1p1x coloured by chain, side view.
PDB entry 1p1x coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Analysis of the class I aldolase binding site architecture based on the crystal structure of 2-deoxyribose-5-phosphate aldolase at 0.99A resolution.
Heine A, Luz JG, Wong CH, Wilson IA
J Mol Biol 343 1019-34 (2004)
PMID: 15476818

Function and Biology Details

Reaction catalysed: 
2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141373 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Deoxyribose-phosphate aldolase Chains: A, B
Molecule details ›
Chains: A, B
Length: 260 amino acids
Theoretical weight: 27.91 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A6L0 (Residues: 1-259; Coverage: 100%)
Gene names: JW4344, b4381, deoC, dra, thyR
Sequence domains: DeoC/LacD family aldolase
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P21
Unit cell:
a: 48.73Å b: 42.01Å c: 145.41Å
α: 90° β: 98.53° γ: 90°
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Physicochemical Properties of Ion Pairs of Biological Macromolecules.
Iwahara et al. (2015)
3 more

9 mentions without citation

Catalytic cycle of human glutathione reductase near 1 A resolution.
Berkholz et al. (2008)
8 more