› 1rv8

X-ray diffraction
2.3Å resolution

Class II fructose-1,6-bisphosphate aldolase from Thermus aquaticus in complex with cobalt

Released:
DOI: 10.2210/pdb1rv8/pdb
PDB entry 1rv8 coloured by chain, front view.
PDB entry 1rv8 coloured by chain, side view.
PDB entry 1rv8 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:
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

3 bound ligands:
Ligand SO4 12 x SO4
Ligand CO 5 x CO
Ligand NA 4 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: P2
Unit cell:
a: 99.354Å b: 57.629Å c: 138.577Å
α: 90° β: 90.23° γ: 90°
R-values:
R R work R free
0.211 0.211 0.252
Expression system: Escherichia coli

Quick links

Citations

25 citation in other articles

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

6 mentions without citation

Combinatorial use of environmental stresses and genetic engineering to increase ethanol titres in cyanobacteria.
Andrews et al. (2021)
5 more