› 3s5o

X-ray diffraction
1.97Å resolution

Crystal Structure of Human 4-hydroxy-2-oxoglutarate Aldolase Bound to Pyruvate

Released:
DOI: 10.2210/pdb3s5o/pdb
PDB entry 3s5o coloured by chain, front view.
PDB entry 3s5o coloured by chain, side view.
PDB entry 3s5o coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria.
Riedel TJ, Johnson LC, Knight J, Hantgan RR, Holmes RP, Lowther WT
PLoS One 6 e26021 (2011)
PMID: 21998747

Function and Biology Details

Reaction catalysed: 
(4R)-4-hydroxy-2-oxoglutarate = pyruvate + glyoxylate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183250 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
4-hydroxy-2-oxoglutarate aldolase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 307 amino acids
Theoretical weight: 32.98 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q86XE5 (Residues: 26-327; Coverage: 92%)
Gene names: C10orf65, DHDPSL, HOGA1
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

2 bound ligands:
Ligand EDO 6 x EDO
Ligand K 1 x K
1 modified residue:
Ligand KPI 1 x KPI

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P6422
Unit cell:
a: 141.23Å b: 141.23Å c: 108.388Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.197 0.196 0.216
Expression system: Escherichia coli

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Citations

8 review citations

Primary hyperoxaluria.
Cochat et al. (2013)
7 more

3 mentions without citation

Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria.
Riedel et al. (2011)
2 more