› 3pk2

X-ray diffraction
1.9Å resolution

Artificial Transfer Hydrogenases for the Enantioselective Reduction of Cyclic Imines

Released:
DOI: 10.2210/pdb3pk2/pdb
PDB entry 3pk2 coloured by chain, front view.
PDB entry 3pk2 coloured by chain, side view.
PDB entry 3pk2 coloured by chain, top view.
Source organism: Streptomyces avidinii
Primary publication:
Artificial transfer hydrogenases for the enantioselective reduction of cyclic imines.
Dürrenberger M, Heinisch T, Wilson YM, Rossel T, Nogueira E, Knörr L, Mutschler A, Kersten K, Zimbron MJ, Pierron J, Schirmer T, Ward TR
Angew Chem Int Ed Engl 50 3026-9 (2011)
PMID: 21404391

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149694 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Streptavidin Chain: A
Molecule details ›
Chain: A
Length: 159 amino acids
Theoretical weight: 16.55 KDa
Source organism: Streptomyces avidinii
Expression system: Escherichia coli
UniProt:
  • Canonical: P22629 (Residues: 38-183; Coverage: 92%)
Sequence domains: Avidin family
Structure domains: Avidin-like

Ligands and Environments

2 bound ligands:
Ligand 4IR 1 x 4IR
Ligand IR3 2 x IR3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06DA
Spacegroup: I4122
Unit cell:
a: 57.616Å b: 57.616Å c: 184.031Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.184 0.204
Expression system: Escherichia coli

Quick links

Citations

10 review citations

Transition metal catalysis in confined spaces.
Leenders et al. (2015)
9 more

3 mentions without citation

Designing Artificial Metalloenzymes by Tuning of the Environment beyond the Primary Coordination Sphere.
Van Stappen et al. (2022)
2 more