› 2gcg

X-ray diffraction
2.2Å resolution

Ternary Crystal Structure of Human Glyoxylate Reductase/Hydroxypyruvate Reductase

Released:
DOI: 10.2210/pdb2gcg/pdb
PDB entry 2gcg coloured by chain, front view.
PDB entry 2gcg coloured by chain, side view.
PDB entry 2gcg 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


Cofactor: Ligand NDP 4 x NDP
2 bound ligands:
Ligand DGY 2 x DGY
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SRS BEAMLINE PX14.1
Spacegroup: P21
Unit cell:
a: 76.568Å b: 66.877Å c: 149.78Å
α: 90° β: 98.22° γ: 90°
R-values:
R R work R free
0.205 0.201 0.282
Expression system: Escherichia coli

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Citations

5 review citations

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

7 mentions without citation

Emodin regulates neutrophil phenotypes to prevent hypercoagulation and lung carcinogenesis.
Li et al. (2019)
6 more