Brand  (β version)

PDB ID: 1IL0

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Ligands
Code Name Style Show Link
CAA Acetoacetyl-coenzyme a PoSSuM
NAD Nicotinamide-adenine-dinucleotide PoSSuM
Non-standard Residues
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Glycosylation
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Structure summary

Code : 1IL0   PDBj   RCSB PDB   PDBe
Header : OXIDOREDUCTASE
Title : X-RAY CRYSTAL STRUCTURE OF THE E170Q MUTANT OF HUMAN L-3-HYDROXYACYL-COA DEHYDROGENASE
Release Data : 2001-11-07
Compound :
mol_id molecule chains synonym
1 3-hydroxyacyl-CoA dehydrogenase A,B HCDH
ec: 1.1.1.35
mutation: E170Q
Source :
mol_id organism_scientific organism_common expression_system
1 Homo sapiens  (taxid:9606) Human Escherichia coli  (taxid:562)
gene: HCDH
expression_system_vector_type: plasmid
expression_system_plasmid: pET28
Authors : Barycki, J.J., O'Brien, L.K., Strauss, A.W., Banaszak, L.J.
Keywords : ABORTIVE TERNARY COMPLEX, OXIDOREDUCTASE
Exp. method : X-RAY DIFFRACTION ( 2.20 Å )
Citation :

Glutamate 170 of human l-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme.

Barycki, J.J.,O'Brien, L.K.,Strauss, A.W.  et al.
(2001)  J.Biol.Chem.  276 : 36718 - 36726

PubMed: 11451959
DOI: 10.1074/jbc.M104839200

Sequestration of the Active Site by Interdomain Shifting. CRYSTALLOGRAPHIC AND SPECTROSCOPIC EVIDENCE FOR DISTINCT CONFORMATIONS OF L-3-HYDROXYACYL-CoA DEHYDROGENASE

Barycki, J.J.,O'Brien, L.K.,Strauss, A.W.  et al.
(2000)  J.Biol.Chem.  275 : 27186 - 27196

Reaction

Chain : A, B
UniProt : Q16836 (HCDH_HUMAN)
Reaction: EC: Evidence:
Physiological Direction:
a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + H(+) + NADH 1.1.1.35 PubMed:10231530, PubMed:11489939, PubMed:16725361
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(3S)-3-hydroxybutanoyl-CoA + NAD(+) = acetoacetyl-CoA + H(+) + NADH - PubMed:10231530, PubMed:16725361
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(3S)-hydroxydecanoyl-CoA + NAD(+) = 3-oxodecanoyl-CoA + H(+) + NADH - UniProtKB:P00348
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(3S)-hydroxyhexadecanoyl-CoA + NAD(+) = 3-oxohexadecanoyl-CoA + H(+) + NADH - UniProtKB:P00348
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