› 5vy5

Electron Microscopy
2.6Å resolution

Rabbit muscle aldolase using 200keV

Released:
DOI: 10.2210/pdb5vy5/pdb
PDB entry 5vy5 coloured by chain, ensemble of 10 models, front view.
PDB entry 5vy5 coloured by chain, ensemble of 10 models, side view.
PDB entry 5vy5 coloured by chain, ensemble of 10 models, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Achieving better-than-3-Å resolution by single-particle cryo-EM at 200 keV.
Herzik MA, Wu M, Lander GC
OpenAccess logo Nat Methods 14 1075-1078 (2017)
PMID: 28991891
Related structures: EMD-8743

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 tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-133666 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fructose-bisphosphate aldolase A Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 363 amino acids
Theoretical weight: 39.26 KDa
Source organism: Oryctolagus cuniculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P00883 (Residues: 2-364; Coverage: 100%)
Gene name: ALDOA
Sequence domains: Fructose-bisphosphate aldolase class-I
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 2.6Å
Relevant EMDB volumes: EMD-8743
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Cryo-EM in drug discovery: achievements, limitations and prospects.
Renaud et al. (2018)
12 more

7 mentions without citation

Achieving better-than-3-Å resolution by single-particle cryo-EM at 200 keV.
Herzik et al. (2017)
6 more