› 1rvg

X-ray diffraction
2Å resolution

crystal structure of class II fructose-bisphosphate aldolase from Thermus aquaticus in complex with Y

Released:
DOI: 10.2210/pdb1rvg/pdb
Model geometry
Fit model/data
Data not deposited
PDB entry 1rvg coloured by chain, front view.
PDB entry 1rvg coloured by chain, side view.
PDB entry 1rvg coloured by chain, top view.
Source organism: Thermus aquaticus
Primary publication:
Induced fit movements and metal cofactor selectivity of class II aldolases: structure of Thermus aquaticus fructose-1,6-bisphosphate aldolase.
Izard T, Sygusch J
J Biol Chem 279 11825-33 (2004)
PMID: 14699122

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193174 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 305 amino acids
Theoretical weight: 33.14 KDa
Source organism: Thermus aquaticus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9RHA2 (Residues: 1-305; Coverage: 100%)
Gene names: BVI061214_00874, fba
Sequence domains: Fructose-bisphosphate aldolase class-II
Structure domains: Aldolase class I

Ligands and Environments

4 bound ligands:
Ligand SO4 11 x SO4
Ligand CO 5 x CO
Ligand NA 4 x NA
Ligand YT3 1 x YT3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P2
Unit cell:
a: 99.86Å b: 57.55Å c: 138.617Å
α: 90° β: 90.26° γ: 90°
R-values:
R R work R free
0.225 0.225 0.259
Expression system: Escherichia coli

Quick links

Citations

28 citation in other articles

Modeling protein quaternary structure of homo- and hetero-oligomers beyond binary interactions by homology.
Bertoni et al. (2017)
27 more

3 mentions without citation

Glycolytic enzyme interactions with yeast and skeletal muscle F-actin.
Waingeh et al. (2006)
2 more