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3QE3

Sheep liver sorbitol dehydrogenase

Summary for 3QE3
Entry DOI10.2210/pdb3qe3/pdb
DescriptorSorbitol dehydrogenase, ZINC ION, GLYCEROL, ... (5 entities in total)
Functional Keywordsmedium chain dehydrogenase/reductase enzymes, oxidoreductase
Biological sourceOvis aries (sheep)
Cellular locationMitochondrion membrane; Peripheral membrane protein: P07846
Total number of polymer chains1
Total formula weight38352.55
Authors
Yennawar, N.H.,Yennawar, H.P. (deposition date: 2011-01-19, release date: 2011-04-27, Last modification date: 2023-09-13)
Primary citationYennawar, H.,Moller, M.,Gillilan, R.,Yennawar, N.
X-ray crystal structure and small-angle X-ray scattering of sheep liver sorbitol dehydrogenase.
Acta Crystallogr.,Sect.D, 67:440-446, 2011
Cited by
PubMed Abstract: The X-ray crystal structure of sheep liver sorbitol dehydrogenase (slSDH) has been determined using the crystal structure of human sorbitol dehydrogenase (hSDH) as a molecular-replacement model. slSDH crystallized in space group I222 with one monomer in the asymmetric unit. A conserved tetramer that superposes well with that seen in hSDH (despite belonging to a different space group) and obeying the 222 crystal symmetry is seen in slSDH. An acetate molecule is bound in the active site, coordinating to the active-site zinc through a water molecule. Glycerol, a substrate of slSDH, also occupies the substrate-binding pocket together with the acetate designed by nature to fit large polyol substrates. The substrate-binding pocket is seen to be in close proximity to the tetramer interface, which explains the need for the structural integrity of the tetramer for enzyme activity. Small-angle X-ray scattering was also used to identify the quaternary structure of the tetramer of slSDH in solution.
PubMed: 21543846
DOI: 10.1107/S0907444911007815
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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