› 2wwr

X-ray diffraction
2.82Å resolution

Crystal Structure of Human Glyoxylate Reductase Hydroxypyruvate Reductase

Released:
DOI: 10.2210/pdb2wwr/pdb
PDB entry 2wwr coloured by chain, front view.
PDB entry 2wwr coloured by chain, side view.
PDB entry 2wwr coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis of substrate specificity in human glyoxylate reductase/hydroxypyruvate reductase.
Booth MP, Conners R, Rumsby G, Brady RL
J Mol Biol 360 178-89 (2006)
PMID: 16756993

Function and Biology Details

Reactions catalysed: 
Glycolate + NADP(+) = glyoxylate + NADPH
D-glycerate + NAD(P)(+) = hydroxypyruvate + NAD(P)H
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193665 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glyoxylate reductase/hydroxypyruvate reductase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 330 amino acids
Theoretical weight: 35.87 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UBQ7 (Residues: 1-328; Coverage: 100%)
Gene names: GLXR, GRHPR, MSTP035
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 67.356Å b: 116.08Å c: 198.23Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.217 0.279
Expression system: Escherichia coli

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Citations

5 review citations

Evolution of rosmarinic acid biosynthesis.
Petersen et al. (2009)
4 more

1 mention without citation

New insights into the mechanism of substrates trafficking in Glyoxylate/Hydroxypyruvate reductases.
Lassalle et al. (2016)