› 2v2a

X-ray diffraction
1.75Å resolution

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT E192A- K248G-R253A-E254A)

Released:
DOI: 10.2210/pdb2v2a/pdb
PDB entry 2v2a coloured by chain, front view.
PDB entry 2v2a coloured by chain, side view.
PDB entry 2v2a coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Antenna domain mobility and enzymatic reaction of L-rhamnulose-1-phosphate aldolase.
Grueninger D, Schulz GE
Biochemistry 47 607-14 (2008)
PMID: 18085797

Function and Biology Details

Reaction catalysed: 
L-rhamnulose 1-phosphate = glycerone phosphate + (S)-lactaldehyde
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-152217 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rhamnulose-1-phosphate aldolase Chain: A
Molecule details ›
Chain: A
Length: 274 amino acids
Theoretical weight: 29.9 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P32169 (Residues: 1-274; Coverage: 100%)
Gene names: JW3873, b3902, rhaD, rhuA
Sequence domains: Class II Aldolase and Adducin N-terminal domain
Structure domains: Class II aldolase/adducin N-terminal domain

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand 13P 1 x 13P
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P4212
Unit cell:
a: 106.302Å b: 106.302Å c: 56.439Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.149 0.147 0.172
Expression system: Escherichia coli

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Citations

1 review citation

A survey of oxidative paracatalytic reactions catalyzed by enzymes that generate carbanionic intermediates: implications for ROS production, cancer etiology, and neurodegenerative diseases.
Bunik et al. (2011)
5 other articles