› 1e4a

X-ray diffraction
2.15Å resolution

L-Fuculose 1-Phosphate Aldolase from Escherichia coli Mutant Del(27)

Released:
DOI: 10.2210/pdb1e4a/pdb
PDB entry 1e4a coloured by chain, front view.
PDB entry 1e4a coloured by chain, side view.
PDB entry 1e4a coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structures of l-fuculose-1-phosphate aldolase mutants outlining motions during catalysis.
Joerger AC, Mueller-Dieckmann C, Schulz GE
J Mol Biol 303 531-43 (2000)
PMID: 11054289

Function and Biology Details

Reaction catalysed: 
L-fuculose 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-532518 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-fuculose phosphate aldolase Chain: P
Molecule details ›
Chain: P
Length: 214 amino acids
Theoretical weight: 23.72 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AB87 (Residues: 1-215; Coverage: 100%)
Gene names: JW2771, b2800, fucA, fucC, prd
Sequence domains: Class II Aldolase and Adducin N-terminal domain
Structure domains: Class II aldolase/adducin N-terminal domain

Ligands and Environments

3 bound ligands:
Ligand SO4 2 x SO4
Ligand BME 1 x BME
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P4212
Unit cell:
a: 93.25Å b: 93.25Å c: 43.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.156 0.156 0.223
Expression system: Escherichia coli

Quick links

Citations

2 review citations

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