› 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 5ira coloured by chain and viewed from the front.
PDB 5ira coloured by chain and viewed from the side.
PDB 5ira coloured by chain and viewed from the top.
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 (2016)
PMID: 27571282

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (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

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Citations

32 review citations

Organometallic catalysis in aqueous and biological environments: harnessing the power of metal carbenes.
Gutiérrez et al. (2022)
31 more

3 mentions without citation

Functional and morphological adaptation in DNA protocells via signal processing prompted by artificial metalloenzymes.
Samanta et al. (2020)
2 more