› 2v9o

X-ray diffraction
1.95Å resolution

L-RHAMNULOSE-1-PHOSPHATE ALDOLASE FROM ESCHERICHIA COLI (MUTANT A87M- T109F-E192A)

Released:
DOI: 10.2210/pdb2v9o/pdb
PDB entry 2v9o coloured by chain, front view.
PDB entry 2v9o coloured by chain, side view.
PDB entry 2v9o coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Designed protein-protein association.
Grueninger D, Treiber N, Ziegler MO, Koetter JW, Schulze MS, Schulz GE
Science 319 206-9 (2008)
PMID: 18187656

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 Chains: A, E
Molecule details ›
Chains: A, E
Length: 274 amino acids
Theoretical weight: 30.22 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

1 bound ligand:
Ligand ZN 6 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P4
Unit cell:
a: 86.193Å b: 86.193Å c: 89.873Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.203 0.249
Expression system: Escherichia coli

Quick links

Citations

20 review citations

Caught in self-interaction: evolutionary and functional mechanisms of protein homooligomerization.
Hashimoto et al. (2011)
19 more