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Open data
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Basic information
Entry | Database: PDB / ID: 1bvu | ||||||
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Title | GLUTAMATE DEHYDROGENASE FROM THERMOCOCCUS LITORALIS | ||||||
![]() | PROTEIN (GLUTAMATE DEHYDROGENASE) | ||||||
![]() | OXIDOREDUCTASE / Thermal Stability | ||||||
Function / homology | ![]() glutamate dehydrogenase [NAD(P)+] activity / glutamate dehydrogenase [NAD(P)+] / amino acid metabolic process / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Baker, P.J. / Britton, K.L. / Yip, K.S. / Stillman, T.J. / Rice, D.W. | ||||||
![]() | ![]() Title: Structure determination of the glutamate dehydrogenase from the hyperthermophile Thermococcus litoralis and its comparison with that from Pyrococcus furiosus Authors: Britton, K.L. / Yip, K.S. / Sedelnikova, S.E. / Stillman, T.J. / Adams, M.W. / Ma, K. / Maeder, D.L. / Robb, F.T. / Tolliday, N. / Vetriani, C. / Rice, D.W. / Baker, P.J. #1: ![]() Title: Protein Thermostability Above 100C: A Key Role for Ionic Interactions Authors: Vetriani, C. / Maeder, D.L. / Tolliday, N. / Yip, K.S.-P. / Stillman, T.J. / Britton, K.L. / Rice, D.W. / Klump, H.H. / Robb, F.T. #2: ![]() Title: Crystallisation of the Glutamate Dehydrogenase from the Hyperthermophilic Archaeon Thermococcus Litoralis Authors: Sedelnikova, S.E. / Yip, K.S.-P. / Stillman, T.J. / Ma, K. / Adams, M.W.W. / Robb, F.T. / Rice, D.W. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 466.7 KB | Display | ![]() |
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PDB format | ![]() | 389.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 417 KB | Display | ![]() |
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Full document | ![]() | 566.8 KB | Display | |
Data in XML | ![]() | 66.8 KB | Display | |
Data in CIF | ![]() | 97.2 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: 46664.219 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: Q56304, glutamate dehydrogenase [NAD(P)+] |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.88 Å3/Da / Density % sol: 57.33 % | |||||||||||||||||||||||||
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Crystal grow | pH: 8 Details: 35MG/ML PROTEIN IN 0.1M HEPES BUFFER PH 8.0 CONTAINING 1.7-1.8M AMMONIUM SULPHATE AND 1.5% W/V PEG 8000. | |||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Resolution: 2.5→20 Å / Num. obs: 101702 / % possible obs: 93 % / Observed criterion σ(I): 0 / Redundancy: 1.7 % / Rmerge(I) obs: 0.042 |
Reflection | *PLUS Num. measured all: 173711 |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 2.5→10 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rwork: 0.192 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |