› 7epr

X-ray diffraction
2.2Å resolution

Partial Consensus L-threonine 3-dehydrogenase (C-Change)

Released:
DOI: 10.2210/pdb7epr/pdb
PDB entry 7epr coloured by chain, front view.
PDB entry 7epr coloured by chain, side view.
PDB entry 7epr coloured by chain, top view.
Source organism: synthetic construct
Primary publication:
Partial Consensus Design and Enhancement of Protein Function by Secondary-Structure-Guided Consensus Mutations.
Kozuka K, Nakano S, Asano Y, Ito S
Biochemistry 60 2309-2319 (2021)
PMID: 34254784

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-168238 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-threonine 3-dehydrogenase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 338 amino acids
Theoretical weight: 37.29 KDa
Source organism: synthetic construct
Expression system: Escherichia coli

Ligands and Environments

1 bound ligand:
Ligand NAD 4 x NAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: C2
Unit cell:
a: 149.019Å b: 58.474Å c: 138.13Å
α: 90° β: 92.234° γ: 90°
R-values:
R R work R free
0.211 0.208 0.258
Expression system: Escherichia coli

Quick links

Citations

1 citations in other articles

Understanding the molecular mechanisms of odorant binding and activation of the human OR52 family.
Choi et al. (2023)