› 6smt

X-ray diffraction
1.55Å resolution

S-enantioselective imine reductase from Mycobacterium smegmatis

Released:
DOI: 10.2210/pdb6smt/pdb
PDB entry 6smt coloured by chain, front view.
PDB entry 6smt coloured by chain, side view.
PDB entry 6smt coloured by chain, top view.
Source organism: Mycolicibacterium smegmatis MC2 155
Primary publication:
Structural Characterization of an S-enantioselective Imine Reductase from Mycobacterium Smegmatis.
Meyer T, Zumbrägel N, Geerds C, Gröger H, Niemann HH
OpenAccess logo Biomolecules 10 (2020)
PMID: 32751900

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-106478 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
6-phosphogluconate dehydrogenase, NAD-binding Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 298 amino acids
Theoretical weight: 31.03 KDa
Source organism: Mycolicibacterium smegmatis MC2 155
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0R5X0 (Residues: 2-292; Coverage: 100%)
Gene name: MSMEG_6341
Sequence domains:

Ligands and Environments

6 bound ligands:
Ligand NDP 5 x NDP
Ligand FMT 12 x FMT
Ligand EDO 3 x EDO
Ligand 2EH 5 x 2EH
Ligand GOL 3 x GOL
Ligand PEG 1 x PEG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PETRA III, EMBL c/o DESY BEAMLINE P13 (MX1)
Unit cell:
a: 117.007Å b: 77.023Å c: 194.485Å
α: 90° β: 90.2° γ: 90°
R-values:
R R work R free
0.132 0.131 0.155
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 citation in other articles

Computational Study of Mechanism and Enantioselectivity of Imine Reductase from Amycolatopsis orientalis.
Prejanò et al. (2022)
3 more

1 mention without citation

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