› 1ojr

X-ray diffraction
1.35Å resolution

L-rhamnulose-1-phosphate aldolase from Escherichia coli (mutant E192A)

Released:
DOI: 10.2210/pdb1ojr/pdb
PDB entry 1ojr coloured by chain, front view.
PDB entry 1ojr coloured by chain, side view.
PDB entry 1ojr coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase.
Kroemer M, Merkel I, Schulz GE
Biochemistry 42 10560-8 (2003)
PMID: 12962479

Function and Biology Details

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

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: 30.12 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

5 bound ligands:
Ligand ZN 1 x ZN
Ligand PO4 2 x PO4
Ligand 2HA 1 x 2HA
Ligand DIO 1 x DIO
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE BW7B
Spacegroup: P4212
Unit cell:
a: 108.024Å b: 108.024Å c: 57.166Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.112 0.111 0.142
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Rubisco is not really so bad.
Bathellier et al. (2018)
4 more

4 mentions without citation

Structural and biochemical basis for the inhibition of cell death by APIP, a methionine salvage enzyme.
Kang et al. (2014)
3 more