3HHP
Malate dehydrogenase open conformation
Summary for 3HHP
| Entry DOI | 10.2210/pdb3hhp/pdb |
| Descriptor | Malate dehydrogenase (2 entities in total) |
| Functional Keywords | malate dehydrogenase, mdh, citric acid cycle, tca cycle, nad, oxidoreductase, tricarboxylic acid cycle |
| Biological source | Escherichia coli K-12 |
| Total number of polymer chains | 4 |
| Total formula weight | 129472.70 |
| Authors | Zaitseva, J.,Meneely, K.M.,Lamb, A.L. (deposition date: 2009-05-15, release date: 2009-09-22, Last modification date: 2024-02-21) |
| Primary citation | Zaitseva, J.,Meneely, K.M.,Lamb, A.L. Structure of Escherichia coli malate dehydrogenase at 1.45 A resolution. Acta Crystallogr.,Sect.F, 65:866-869, 2009 Cited by PubMed Abstract: The structure of apo malate dehydrogenase from Escherichia coli has been determined to 1.45 A resolution. The crystals belonged to space group C2, with unit-cell parameters a = 146.0, b = 52.0, c = 168.9 A, beta = 102.2 degrees. The structure was determined with the molecular-replacement pipeline program BALBES and was refined to a final R factor of 18.6% (R(free) = 21.4%). The final model has two dimers in the asymmetric unit. In each dimer one monomer contains the active-site loop in the open conformation, whereas in the opposing monomer the active-site loop is disordered. PubMed: 19724119DOI: 10.1107/S1744309109032217 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.45 Å) |
Structure validation
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