1gt7

X-ray diffraction
2.7Å resolution

L-rhamnulose-1-phosphate aldolase from Escherichia coli

Released:
Source organism: Escherichia coli

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 octamer (preferred)
PDBe Complex ID:
PDB-CPX-152218 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rhamnulose-1-phosphate aldolase Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T
Length: 274 amino acids
Theoretical weight: 30.17 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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X11
Spacegroup: P3221
Unit cell:
a: 225.76Å b: 225.76Å c: 285.645Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.233 0.233 0.235
Expression system: Escherichia coli