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PDBsum entry 3s5o
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PDB id:
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Lyase
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Title:
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Crystal structure of human 4-hydroxy-2-oxoglutarate aldolase bound to pyruvate
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Structure:
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4-hydroxy-2-oxoglutarate aldolase, mitochondrial. Chain: a. Synonym: dihydrodipicolinate synthase-like, dhdps-like protein, 2- keto-4-hydroxyglutarate aldolase, khg-aldolase, protein 569272. Engineered: yes
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Source:
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Homo sapiens. Human. Organism_taxid: 9606. Gene: c10orf65, dhdpsl, hoga1. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Resolution:
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1.97Å
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R-factor:
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0.197
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R-free:
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0.216
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Authors:
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T.J.Riedel,W.T.Lowther
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Key ref:
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T.J.Riedel
et al.
(2011).
Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria.
Plos One,
6,
e26021.
PubMed id:
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Date:
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23-May-11
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Release date:
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26-Oct-11
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PROCHECK
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Headers
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References
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Q86XE5
(HOGA1_HUMAN) -
4-hydroxy-2-oxoglutarate aldolase, mitochondrial from Homo sapiens
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Seq: Struc:
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327 a.a.
296 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 1 residue position (black
cross)
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Enzyme class:
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E.C.4.1.3.16
- 4-hydroxy-2-oxoglutarate aldolase.
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Reaction:
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1.
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(4R)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate
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2.
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(4S)-4-hydroxy-2-oxoglutarate = glyoxylate + pyruvate
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(4R)-4-hydroxy-2-oxoglutarate
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glyoxylate
Bound ligand (Het Group name = )
matches with 80.00% similarity
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pyruvate
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(4S)-4-hydroxy-2-oxoglutarate
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=
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glyoxylate
Bound ligand (Het Group name = )
matches with 80.00% similarity
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+
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pyruvate
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Plos One
6:e26021
(2011)
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PubMed id:
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Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria.
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T.J.Riedel,
L.C.Johnson,
J.Knight,
R.R.Hantgan,
R.P.Holmes,
W.T.Lowther.
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ABSTRACT
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');
}
}
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