3S5N

Crystal Structure of Human 4-hydroxy-2-oxoglutarate Aldolase

Summary for 3S5N

Entry DOI	10.2210/pdb3s5n/pdb
Related	3S5O
Descriptor	4-hydroxy-2-oxoglutarate aldolase, mitochondrial, POTASSIUM ION, SODIUM ION, ... (5 entities in total)
Functional Keywords	aldolase, beta barrel, hydroxyproline metabolism, lyase
Biological source	Homo sapiens (human)
Cellular location	Mitochondrion (By similarity): Q86XE5
Total number of polymer chains	1
Total formula weight	33087.95
Authors	Riedel, T.J.,Lowther, W.T. (deposition date: 2011-05-23, release date: 2011-10-26, Last modification date: 2024-02-28)
Primary citation	Riedel, T.J.,Johnson, L.C.,Knight, J.,Hantgan, R.R.,Holmes, R.P.,Lowther, W.T. Structural and Biochemical Studies of Human 4-hydroxy-2-oxoglutarate Aldolase: Implications for Hydroxyproline Metabolism in Primary Hyperoxaluria. Plos One, 6:e26021-e26021, 2011 Cited by PubMed Abstract: 4-hydroxy-2-oxoglutarate (HOG) aldolase is a unique enzyme in the hydroxyproline degradation pathway catalyzing the cleavage of HOG to pyruvate and glyoxylate. Mutations in this enzyme are believed to be associated with the excessive production of oxalate in primary hyperoxaluria type 3 (PH3), although no experimental data is available to support this hypothesis. Moreover, the identity, oligomeric state, enzymatic activity, and crystal structure of human HOGA have not been experimentally determined. PubMed: 21998747 DOI: 10.1371/journal.pone.0026021 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.5 Å)

Structure validation