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Open data
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Basic information
Entry | Database: PDB / ID: 1hrd | ||||||
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Title | GLUTAMATE DEHYDROGENASE | ||||||
![]() | GLUTAMATE DEHYDROGENASE | ||||||
![]() | OXIDOREDUCTASE / NAD | ||||||
Function / homology | ![]() glutamate catabolic process via 2-hydroxyglutarate / glutamate dehydrogenase / glutamate biosynthetic process / glutamate dehydrogenase (NADP+) activity / glutamate dehydrogenase (NAD+) activity / amino acid metabolic process / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Britton, K.L. / Baker, P.J. / Stillman, T.J. / Rice, D.W. | ||||||
![]() | ![]() Title: The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Authors: 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. #1: ![]() Title: Subunit Assembly and Active Site Location in the Structure of Glutamate Dehydrogenase Authors: Baker, P.J. / Britton, K.L. / Engel, P.C. / Farrants, G.W. / Lilley, K.S. / Rice, D.W. / Stillman, T.J. #2: ![]() Title: Structural Consequences of Sequence Patterns in the Fingerprint Region of the Nucleotide Binding Fold. Implications for Nucleotide Specificity Authors: Baker, P.J. / Britton, K.L. / Rice, D.W. / Rob, A. / Stillman, T.J. #3: ![]() Title: Structural Relationship between the Hexameric and Tetrameric Family of Glutamate Dehydrogenases Authors: Britton, K.L. / Baker, P.J. / Rice, D.W. / Stillman, T.J. #4: ![]() Title: Crystallization of an Nad+-Dependent Glutamate Dehydrogenase from Clostridium Symbiosum Authors: Rice, D.W. / Hornby, D.P. / Engel, P.C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 271.6 KB | Display | ![]() |
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PDB format | ![]() | 220.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 385.5 KB | Display | ![]() |
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Full document | ![]() | 437.5 KB | Display | |
Data in XML | ![]() | 31.5 KB | Display | |
Data in CIF | ![]() | 50 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 49215.648 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.62 Å3/Da / Density % sol: 45 % |
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: FILM / Detector: FILM / Date: 1987 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Num. obs: 96327 / % possible obs: 88 % / Observed criterion σ(I): 0 / Redundancy: 3.6 % / Rmerge(I) obs: 0.14 |
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Processing
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Refinement | Resolution: 1.96→37.8 Å / σ(F): 0 Details: TNT MEAN B (A**2) : 33.797 RMS CO-ORDINATE SHIFT IN FINAL CYCLE (A) : 0.008
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Refinement step | Cycle: LAST / Resolution: 1.96→37.8 Å
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Refine LS restraints |
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