› 5ira

X-ray diffraction
1.5Å resolution

Expanding Nature's Catalytic Repertoire -Directed Evolution of an Artificial Metalloenzyme for In Vivo Metathesis

Released:
DOI: 10.2210/pdb5ira/pdb
PDB entry 5ira coloured by chain, front view.
PDB entry 5ira coloured by chain, side view.
PDB entry 5ira coloured by chain, top view.
Source organism: Streptomyces avidinii
Primary publication:
Directed evolution of artificial metalloenzymes for in vivo metathesis.
Jeschek M, Reuter R, Heinisch T, Trindler C, Klehr J, Panke S, Ward TR
Nature 537 661-665 (2016)
PMID: 27571282

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-165822 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Artificial Metathesase Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 16.57 KDa
Source organism: Streptomyces avidinii
Expression system: Escherichia coli
Structure domains: Avidin-like

Ligands and Environments

1 bound ligand:
Ligand 9RU 1 x 9RU
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: I4122
Unit cell:
a: 57.496Å b: 57.496Å c: 183.415Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.137 0.135 0.174
Expression system: Escherichia coli

Quick links

Citations

38 review citations

Biocatalysis: Enzymatic Synthesis for Industrial Applications.
Wu et al. (2021)
37 more

3 mentions without citation

Artificial Metalloenzymes Based on the Biotin-Streptavidin Technology: Enzymatic Cascades and Directed Evolution.
Liang et al. (2019)
2 more