5k4u

X-ray diffraction
1.9Å resolution

Three-dimensional structure of L-threonine 3-dehydrogenase from Trypanosoma brucei showing different active site loop conformations between dimer subunits, refined to 1.9 angstroms

Released:
Model geometry
Fit model/data

Function and Biology Details

Reaction catalysed:
L-threonine + NAD(+) = L-2-amino-3-oxobutanoate + NADH
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-182221 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-threonine 3-dehydrogenase, mitochondrial Chains: A, C
Molecule details ›
Chains: A, C
Length: 320 amino acids
Theoretical weight: 35.71 KDa
Source organism: Trypanosoma brucei
Expression system: Escherichia coli
UniProt:
  • Canonical: Q7YW97 (Residues: 14-332; Coverage: 100%)
Sequence domains: NAD dependent epimerase/dehydratase family
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments


Cofactor: Ligand NAD 2 x NAD
2 bound ligands:
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: DIAMOND BEAMLINE I04-1
Spacegroup: P21212
Unit cell:
a: 90.074Å b: 133.095Å c: 55.606Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.223
Expression system: Escherichia coli