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1HRD

GLUTAMATE DEHYDROGENASE

Summary for 1HRD
Entry DOI10.2210/pdb1hrd/pdb
DescriptorGLUTAMATE DEHYDROGENASE (2 entities in total)
Functional Keywordsoxidoreductase, nad
Biological sourceClostridium symbiosum
Total number of polymer chains3
Total formula weight147646.94
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 citationYip, 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: 8591026
DOI: 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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