› 2q50

X-ray diffraction
2.45Å resolution

Ensemble refinement of the protein crystal structure of a glyoxylate/hydroxypyruvate reductase from Homo sapiens

Released:
DOI: 10.2210/pdb2q50/pdb
PDB 2q50 coloured by chain and viewed from the front.
PDB 2q50 coloured by chain and viewed from the side.
PDB 2q50 coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Ensemble refinement of protein crystal structures: validation and application.
Levin EJ, Kondrashov DA, Wesenberg GE, Phillips GN
Structure 15 1040-52 (2007)
PMID: 17850744

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (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:
Ligand MSE 20 x MSE

Experiments and Validation Details

Entry percentile scores
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
0.2 0.2 0.286
Expression system: Escherichia coli

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Citations

18 review citations

Bringing diffuse X-ray scattering into focus.
Wall et al. (2018)
17 more