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- PDB-7d97: Crystal structure of N109P mutant of GATase subunit of Methanocal... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7d97 | |||||||||
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Title | Crystal structure of N109P mutant of GATase subunit of Methanocaldococcus jannaschii GMP synthetase | |||||||||
![]() | GMP synthase [glutamine-hydrolyzing] subunit A | |||||||||
![]() | LIGASE / hyperthermostable glutamine amidotransferase / GATase_N109P | |||||||||
Function / homology | ![]() GMP synthase activity / GMP synthase (glutamine-hydrolysing) / glutamine metabolic process / ATP binding / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() | |||||||||
![]() | Bellur, A. / Dongre, A. / Kavya, J. / Balaram, H. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for the hyperthermostability of an archaeal enzyme induced by succinimide formation. Authors: Dongre, A.V. / Das, S. / Bellur, A. / Kumar, S. / Chandrashekarmath, A. / Karmakar, T. / Balaram, P. / Balasubramanian, S. / Balaram, H. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 164 KB | Display | ![]() |
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PDB format | ![]() | 126.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 451.7 KB | Display | ![]() |
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Full document | ![]() | 461.4 KB | Display | |
Data in XML | ![]() | 34.2 KB | Display | |
Data in CIF | ![]() | 50 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7d40SC ![]() 7d95C ![]() 7d96C S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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3 | ![]()
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4 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 21034.262 Da / Num. of mol.: 4 / Mutation: N109P Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: DSM 2661 / Gene: guaAA, MJ1575 / Production host: ![]() ![]() References: UniProt: Q58970, GMP synthase (glutamine-hydrolysing) #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 43.12 % |
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Crystal grow | Temperature: 277 K / Method: microbatch / pH: 5.6 / Details: 100 mM Sodium acetate, pH 5.6, 20 % PEG 3350 |
-Data collection
Diffraction | Mean temperature: 277 K / Serial crystal experiment: N | |||||||||||||||||||||||||
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Diffraction source | Source: ![]() | |||||||||||||||||||||||||
Detector | Type: MAR scanner 345 mm plate / Detector: IMAGE PLATE / Date: Feb 17, 2020 | |||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1.54179 Å / Relative weight: 1 | |||||||||||||||||||||||||
Reflection twin |
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Reflection | Resolution: 1.89→35.49 Å / Num. obs: 48293 / % possible obs: 93.7 % / Redundancy: 2.1 % / CC1/2: 0.861 / Net I/σ(I): 1.28 | |||||||||||||||||||||||||
Reflection shell | Resolution: 1.89→2.03 Å / Num. unique obs: 5717 / CC1/2: 0.702 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 7D40 Resolution: 1.89→35.49 Å / Cor.coef. Fo:Fc: 0.873 / Cor.coef. Fo:Fc free: 0.821 / SU B: 4.223 / SU ML: 0.126 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.048 / ESU R Free: 0.042 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 47.12 Å2 / Biso mean: 12.344 Å2 / Biso min: 2.62 Å2
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Refinement step | Cycle: final / Resolution: 1.89→35.49 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.89→1.937 Å / Rfactor Rfree error: 0 |