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Open data
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Basic information
Entry | Database: PDB / ID: 1gtm | ||||||
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Title | STRUCTURE OF GLUTAMATE DEHYDROGENASE | ||||||
![]() | GLUTAMATE DEHYDROGENASE | ||||||
![]() | OXIDOREDUCTASE / NAD / NADP | ||||||
Function / homology | ![]() glutamate dehydrogenase [NAD(P)+] activity / glutamate dehydrogenase [NAD(P)+] / amino acid metabolic process / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Yip, K.S.P. / Stillman, T.J. / Britton, K.L. / Pasquo, A. / 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: Insights Into Thermal Stability from a Comparison of the Glutamate Dehydrogenases from Pyrococcus Furiosus and Thermococcus Litoralis Authors: Britton, K.L. / Baker, P.J. / Borges, K.M. / Engel, P.C. / Pasquo, A. / Rice, D.W. / Robb, F.T. / Scandurra, R. / Stillman, T.J. / Yip, K.S. #2: ![]() Title: Crystallisation of the Nad(P)-Dependent Glutamate Dehydrogenase from the Hyperthermophile Pyrococcus Furiosus Authors: Yip, K.S.P. / Stillman, T.J. / Baker, P.J. / Britton, K.L. / Engel, P.C. / Sedelnikova, S.E. / Rice, D.W. / Pasquo, A. / Chiaraluce, R. / Consalvi, V. / Scandurra, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 252.7 KB | Display | ![]() |
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PDB format | ![]() | 206.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 405.1 KB | Display | ![]() |
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Full document | ![]() | 462 KB | Display | |
Data in XML | ![]() | 31 KB | Display | |
Data in CIF | ![]() | 47.5 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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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 46982.590 Da / Num. of mol.: 3 / Source method: isolated from a natural source / Source: (natural) ![]() ![]() References: UniProt: P80319, glutamate dehydrogenase [NAD(P)+] #2: Chemical | ChemComp-SO4 / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 4.28 Å3/Da / Density % sol: 67.4 % | ||||||||||||||||||||
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Crystal | *PLUS | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 290 K / pH: 7.5 / Method: vapor diffusion, hanging dropDetails: Yip, K.S.P., (1995) Acta Crystallogr.,Sect.D, 51, 240. | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Sep 1, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.92 Å / Relative weight: 1 |
Reflection | Num. obs: 115181 / % possible obs: 93.2 % / Observed criterion σ(I): 0 / Redundancy: 2.6 % / Rmerge(I) obs: 0.043 |
Reflection | *PLUS Highest resolution: 2.2 Å / Redundancy: 2.58 % |
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Processing
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Refinement | Resolution: 2.2→10 Å
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Refinement step | Cycle: LAST / Resolution: 2.2→10 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Num. reflection obs: 115153 / Rfactor obs: 0.17 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 38 Å2 | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: t_angle_deg / Dev ideal: 2.85 |