› 4ald

X-ray diffraction
2.8Å resolution

HUMAN MUSCLE FRUCTOSE 1,6-BISPHOSPHATE ALDOLASE COMPLEXED WITH FRUCTOSE 1,6-BISPHOSPHATE

Released:
DOI: 10.2210/pdb4ald/pdb
PDB entry 4ald coloured by chain, front view.
PDB entry 4ald coloured by chain, side view.
PDB entry 4ald coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of human muscle aldolase complexed with fructose 1,6-bisphosphate: mechanistic implications.
Dalby A, Dauter Z, Littlechild JA
Protein Sci 8 291-7 (1999)
PMID: 10048322

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 domain:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137391 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase A Chain: A
Molecule details ›
Chain: A
Length: 363 amino acids
Theoretical weight: 39.34 KDa
Source organism: Homo sapiens
UniProt:
  • Canonical: P04075 (Residues: 2-364; Coverage: 100%)
Gene names: ALDA, ALDOA
Sequence domains: Fructose-bisphosphate aldolase class-I
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand 2FP 1 x 2FP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P6422
Unit cell:
a: 96.5Å b: 96.5Å c: 166.9Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.202 0.202 0.304

Quick links

Citations

3 review citations

Glycolysis as a target for the design of new anti-trypanosome drugs.
Verlinde et al. (2001)
2 more

16 mentions without citation

Aldolase provides an unusual binding site for thrombospondin-related anonymous protein in the invasion machinery of the malaria parasite.
Bosch et al. (2007)
15 more