4a22

X-ray diffraction
1.9Å resolution

Structure of Mycobacterium tuberculosis fructose 1,6-bisphosphate aldolase bound to N-(4-hydroxybutyl)- glycolohydroxamic acid bis- phosphate

Released:

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
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

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2
Unit cell:
a: 335.386Å b: 42.977Å c: 102.601Å
α: 90° β: 99.39° γ: 90°
R-values:
R R work R free
0.182 0.179 0.221
Expression system: Escherichia coli BL21(DE3)