1HRD
GLUTAMATE DEHYDROGENASE
Summary for 1HRD
| Entry DOI | 10.2210/pdb1hrd/pdb |
| Descriptor | GLUTAMATE DEHYDROGENASE (2 entities in total) |
| Functional Keywords | oxidoreductase, nad |
| Biological source | Clostridium symbiosum |
| Total number of polymer chains | 3 |
| Total formula weight | 147646.94 |
| Authors | Britton, K.L.,Baker, P.J.,Stillman, T.J.,Rice, D.W. (deposition date: 1996-04-03, release date: 1997-03-12, Last modification date: 2024-02-07) |
| Primary citation | Yip, K.S.,Stillman, T.J.,Britton, K.L.,Artymiuk, P.J.,Baker, P.J.,Sedelnikova, S.E.,Engel, P.C.,Pasquo, A.,Chiaraluce, R.,Consalvi, V.,Scandurra, R.,Rice, D.W. The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure, 3:1147-1158, 1995 Cited by PubMed Abstract: The hyperthermophile Pyrococcus furiosus is one of the most thermostable organisms known, with an optimum growth temperature of 100 degrees C. The proteins from this organism display extreme thermostability. We have undertaken the structure determination of glutamate dehydrogenase from P. furiosus in order to gain further insights into the relationship between molecular structure and thermal stability. PubMed: 8591026DOI: 10.1016/S0969-2126(01)00251-9 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.96 Å) |
Structure validation
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