› 4moz

X-ray diffraction
2.15Å resolution

Fructose-bisphosphate aldolase from Slackia heliotrinireducens DSM 20476

Released:
DOI: 10.2210/pdb4moz/pdb
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PDB entry 4moz coloured by chain, front view.
PDB entry 4moz coloured by chain, side view.
PDB entry 4moz coloured by chain, top view.
Source organism: Slackia heliotrinireducens DSM 20476
Entry authors: Chang C, Li H, Jedrzejczak R, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed: 
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo pentamer (preferred)
homo decamer
Assembly name:
PDBe Complex ID:
PDB-CPX-111729 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
fructose-bisphosphate aldolase Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 319 amino acids
Theoretical weight: 34.6 KDa
Source organism: Slackia heliotrinireducens DSM 20476
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: C7N7V8 (Residues: 1-313; Coverage: 100%)
Gene name: Shel_19790
Sequence domains: DeoC/LacD family aldolase
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 35 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: C2221
Unit cell:
a: 135.783Å b: 174.202Å c: 203.023Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.172 0.169 0.223
Expression system: Escherichia coli BL21(DE3)

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