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Open data
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Basic information
Entry | Database: PDB / ID: 1bgv | ||||||
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Title | GLUTAMATE DEHYDROGENASE | ||||||
![]() | GLUTAMATE DEHYDROGENASE | ||||||
![]() | OXIDOREDUCTASE | ||||||
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 | ![]() ![]() ![]() | ||||||
![]() | Stillman, T.J. / Baker, P.J. / Britton, K.L. / Rice, D.W. | ||||||
![]() | ![]() Title: Conformational flexibility in glutamate dehydrogenase. Role of water in substrate recognition and catalysis. Authors: Stillman, T.J. / Baker, P.J. / Britton, K.L. / Rice, D.W. #1: ![]() Title: Determinants of Substrate Specificity in the Superfamily of Amino Acid Dehydrogenases Authors: Baker, P.J. / Waugh, M.L. / Wang, X.G. / Stillman, T.J. / Turnbull, A.P. / Engel, P.C. / Rice, D.W. #2: ![]() 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. #3: ![]() Title: Erratum. 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. #4: ![]() 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. #5: ![]() 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. #6: ![]() 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. #7: ![]() 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 | ![]() | 102.5 KB | Display | ![]() |
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PDB format | ![]() | 78.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 383.4 KB | Display | ![]() |
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Full document | ![]() | 396.8 KB | Display | |
Data in XML | ![]() | 12 KB | Display | |
Data in CIF | ![]() | 19 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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
#1: Protein | Mass: 49215.648 Da / Num. of mol.: 1 / Source method: isolated from a natural source Details: THE RESIDUE LABELLED B 501, A GLUTAMATE, IS THE ENZYME'S SUBSTRATE WHICH IS BOUND WITHIN THE ACTIVE SITE. IT IS THOUGHT TO AN ONLY PARTIALLY OCCUPIED SITE AND SO ITS OCCUPANCY WAS SET TO 0.53. Source: (natural) ![]() |
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#2: Chemical | ChemComp-GLU / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 54 % |
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Crystal grow | pH: 7 / Details: pH 7.0 |
-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Detector: FILM / Date: Oct 7, 1991 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.88 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→40 Å / Num. obs: 42325 / % possible obs: 99 % / Observed criterion σ(I): 0 / Redundancy: 3.36 % / Rmerge(I) obs: 0.07 |
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Processing
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Refinement | Method to determine structure: ![]() Details: THE RESIDUE LABELLED B 501, A GLUTAMATE, IS THE ENZYME'S SUBSTRATE WHICH IS BOUND WITHIN THE ACTIVE SITE. IT IS THOUGHT TO AN ONLY PARTIALLY OCCUPIED SITE AND SO ITS OCCUPANCY WAS SET TO 0.53.
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Solvent computation | Solvent model: MOEWS AND KRETSINGER / Bsol: 248 Å2 / ksol: 0.85 e/Å3 | ||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.9→10 Å
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Refine LS restraints |
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