1ojr

X-ray diffraction
1.35Å resolution

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

Released:
Source organism: Escherichia coli
Primary publication:
Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase.
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:

Structure analysis Details

Assembly composition:
homo tetramer (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

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