4gh5

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Crystal structure of S-2-hydroxypropyl coenzyme M dehydrogenase (S-HPCDH)Crystal structure of S-2-hydroxypropyl coenzyme M dehydrogenase (S-HPCDH)

Structural highlights

4gh5 is a 4 chain structure with sequence from Xanthobacter autotrophicus Py2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.6Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

HCDS3_XANP2 Involved in aliphatic epoxide carboxylation (PubMed:20302306). Catalyzes the reversible oxidation of (2S)-2-hydroxypropyl-coenzyme M (S-HPC) to 2-oxopropyl-coenzyme M (2-KPC) (PubMed:20302306). The enzyme is highly specific for the S enantiomers (PubMed:20302306). In vitro can also use the aliphatic ketone 2-butanone and the aliphatic alcohol 2-propanol, and shows an inherent stereoselectivity for 2-butanone reduction (PubMed:20302306).[1]

References

  1. Sliwa DA, Krishnakumar AM, Peters JW, Ensign SA. Molecular basis for enantioselectivity in the (R)- and (S)-hydroxypropylthioethanesulfonate dehydrogenases, a unique pair of stereoselective short-chain dehydrogenases/reductases involved in aliphatic epoxide carboxylation. Biochemistry. 2010 Apr 27;49(16):3487-98. doi: 10.1021/bi100294m. PMID:20302306 doi:http://dx.doi.org/10.1021/bi100294m

4gh5, resolution 1.60Å

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OCA