1QOR
CRYSTAL STRUCTURE OF ESCHERICHIA COLI QUINONE OXIDOREDUCTASE COMPLEXED WITH NADPH
Summary for 1QOR
Entry DOI | 10.2210/pdb1qor/pdb |
Descriptor | QUINONE OXIDOREDUCTASE, SULFATE ION, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ... (4 entities in total) |
Functional Keywords | oxidoreductase |
Biological source | Escherichia coli |
Total number of polymer chains | 2 |
Total formula weight | 72109.13 |
Authors | Thorn, J.M.,Barton, J.D.,Dixon, N.E.,Ollis, D.L.,Edwards, K.J. (deposition date: 1995-02-14, release date: 1995-06-03, Last modification date: 2024-02-14) |
Primary citation | Thorn, J.M.,Barton, J.D.,Dixon, N.E.,Ollis, D.L.,Edwards, K.J. Crystal structure of Escherichia coli QOR quinone oxidoreductase complexed with NADPH. J.Mol.Biol., 249:785-799, 1995 Cited by PubMed Abstract: The crystal structure of the homodimer of quinone oxidoreductase from Escherichia coli has been determined using the multiple isomorphous replacement method at 2.2 A resolution and refined to an R-factor of 14.1% The crystallographic asymmetric unit contains one functional dimer with the two subunits being related by a non-crystallographic 2-fold symmetry axis. The model consists of two polypeptide chains (residues 2 through 327), one NADPH molecule and one sulphate anion per subunit, and 432 water molecules. Each subunit consists of two domains: a catalytic domain and a nucleotide-binding domain with the NADPH co-factor bound in the cleft between domains. Quinone oxidoreductase has an unusual nucleotide-binding fingerprint motif consisting of the sequence AXXGXXG. The overall structure of quinone oxidoreductase shows strong structural homology to that of horse liver alcohol dehydrogenase. PubMed: 7602590DOI: 10.1006/jmbi.1995.0337 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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