› 4d3s

X-ray diffraction
2.24Å resolution

Function and Biology Details

Reaction catalysed: 
5,6,7,8-tetrahydrofolate + NADP(+) = 7,8-dihydrofolate + NADPH
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102237 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Imine reductase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 293 amino acids
Theoretical weight: 30.76 KDa
Source organism: Nocardiopsis halophila
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0J9X1X6 (Residues: 1-293; Coverage: 100%)
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand BOG 2 x BOG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21212
Unit cell:
a: 141.17Å b: 153.92Å c: 105.57Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.23 0.266
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

7 review citations

Imine reductases (IREDs).
Mangas-Sanchez et al. (2017)
6 more

2 mentions without citation

Structural Characterization of an S-enantioselective Imine Reductase from Mycobacterium Smegmatis.
Meyer et al. (2020)
1 more