› 5ocm

X-ray diffraction
1.81Å resolution

Imine Reductase from Streptosporangium roseum in complex with NADP+ and 2,2,2-trifluoroacetophenone hydrate

Released:
DOI: 10.2210/pdb5ocm/pdb
PDB 5ocm coloured by chain and viewed from the front.
PDB 5ocm coloured by chain and viewed from the side.
PDB 5ocm coloured by chain and viewed from the top.
Source organism: Streptosporangium roseum
Primary publication:
New imine-reducing enzymes from β-hydroxyacid dehydrogenases by single amino acid substitutions.
Lenz M, Fademrecht S, Sharma M, Pleiss J, Grogan G, Nestl BM
Protein Eng Des Sel 31 109-120 (2018)
PMID: 29733377

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
NAD_binding_2 domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 291 amino acids
Theoretical weight: 30.04 KDa
Source organism: Streptosporangium roseum
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: D2B7Z8 (Residues: 1-291; Coverage: 100%)
Gene name: Sros_0924
Sequence domains: NAD binding domain of 6-phosphogluconate dehydrogenase
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand NAP 6 x NAP
Ligand 9RH 6 x 9RH
Ligand MG 7 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2221
Unit cell:
a: 92.811Å b: 152.434Å c: 251.598Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.168 0.196
Expression system: Escherichia coli BL21(DE3)

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Citations

4 citation in other articles

Characterization of imine reductases in reductive amination for the exploration of structure-activity relationships.
Montgomery et al. (2020)
3 more