› 4a21

X-ray diffraction
2.35Å resolution

Function and Biology Details

Reaction catalysed: 
D-fructose 1,6-bisphosphate = glycerone phosphate + D-glyceraldehyde 3-phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-162056 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 344 amino acids
Theoretical weight: 36.59 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P9WQA3 (Residues: 1-344; Coverage: 100%)
Gene names: MTCY13E10.25c, Rv0363c, fba
Sequence domains: Fructose-bisphosphate aldolase class-II
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand SO4 8 x SO4
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 336.945Å b: 43.234Å c: 103.02Å
α: 90° β: 99.57° γ: 90°
R-values:
R R work R free
0.215 0.211 0.261
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Bacterial plasminogen receptors: mediators of a multifaceted relationship.
Sanderson-Smith et al. (2012)
6 more

3 mentions without citation

Glycolytic and non-glycolytic functions of Mycobacterium tuberculosis fructose-1,6-bisphosphate aldolase, an essential enzyme produced by replicating and non-replicating bacilli.
de la Paz Santangelo et al. (2011)
2 more