2h1s

X-ray diffraction
2.45Å resolution

Crystal Structure of a Glyoxylate/Hydroxypyruvate reductase from Homo sapiens

Released:
Source organism: Homo sapiens
Entry authors: Bitto E, Wesenberg GE, Phillips Jr GN, Bingman CA, Center for Eukaryotic Structural Genomics (CESG)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
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: 328 amino acids
Theoretical weight: 35.9 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9UBQ7 (Residues: 2-328; Coverage: 100%)
Gene names: GLXR, GRHPR, MSTP035
Sequence domains:
Structure domains: NAD(P)-binding Rossmann-like Domain

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 23-ID-D
Spacegroup: P21
Unit cell:
a: 75.996Å b: 66.436Å c: 148.774Å
α: 90° β: 98.59° γ: 90°
R-values:
R R work R free
0.21 0.207 0.264
Expression system: Escherichia coli