2HLP
CRYSTAL STRUCTURE OF THE E267R MUTANT OF A HALOPHILIC MALATE DEHYDROGENASE IN THE APO FORM
Summary for 2HLP
Entry DOI | 10.2210/pdb2hlp/pdb |
Descriptor | MALATE DEHYDROGENASE, CHLORIDE ION, SODIUM ION, ... (4 entities in total) |
Functional Keywords | halophilic, ion-binding, salt bridges, malate dehydrogenase, oxidoreductase |
Biological source | Haloarcula marismortui |
Cellular location | Cytoplasm: Q07841 |
Total number of polymer chains | 2 |
Total formula weight | 65563.12 |
Authors | Richard, S.B.,Madern, D.,Garcin, E.,Zaccai, G. (deposition date: 1999-04-23, release date: 2000-02-04, Last modification date: 2023-08-30) |
Primary citation | Richard, S.B.,Madern, D.,Garcin, E.,Zaccai, G. Halophilic adaptation: novel solvent protein interactions observed in the 2.9 and 2.6 A resolution structures of the wild type and a mutant of malate dehydrogenase from Haloarcula marismortui. Biochemistry, 39:992-1000, 2000 Cited by PubMed: 10653643DOI: 10.1021/bi991001a PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.59 Å) |
Structure validation
Download full validation report