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- PDB-1hto: CRYSTALLOGRAPHIC STRUCTURE OF A RELAXED GLUTAMINE SYNTHETASE FROM... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1hto | ||||||
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Title | CRYSTALLOGRAPHIC STRUCTURE OF A RELAXED GLUTAMINE SYNTHETASE FROM MYCOBACTERIUM TUBERCULOSIS | ||||||
![]() | GLUTAMINE SYNTHETASE | ||||||
![]() | LIGASE / glutamine synthetase / Mycobacterium tuberculosis / Citrate / Structural Genomics / PSI / Protein Structure Initiative / TB Structural Genomics Consortium / TBSGC | ||||||
Function / homology | ![]() nitrogen utilization / positive regulation of plasminogen activation / glutamine synthetase / glutamine biosynthetic process / glutamine synthetase activity / zymogen binding / fibronectin binding / peptidoglycan-based cell wall / protein homooligomerization / magnesium ion binding ...nitrogen utilization / positive regulation of plasminogen activation / glutamine synthetase / glutamine biosynthetic process / glutamine synthetase activity / zymogen binding / fibronectin binding / peptidoglycan-based cell wall / protein homooligomerization / magnesium ion binding / extracellular region / ATP binding / membrane / metal ion binding / plasma membrane / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gill, H.S. / Eisenberg, D. / TB Structural Genomics Consortium (TBSGC) | ||||||
![]() | ![]() Title: Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation. Authors: Gill, H.S. / Pfluegl, G.M. / Eisenberg, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 2.3 MB | Display | ![]() |
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PDB format | ![]() | 1.9 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 5.4 MB | Display | ![]() |
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Full document | ![]() | 5.8 MB | Display | |
Data in XML | ![]() | 507.5 KB | Display | |
Data in CIF | ![]() | 669.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1htqC ![]() 1f52S C: citing same article ( S: Starting model for refinement |
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Similar structure data | |
Other databases |
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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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Unit cell |
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Details | The biological complex is a dodecamer. |
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Components
#1: Protein | Mass: 53496.531 Da / Num. of mol.: 24 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q10377, UniProt: P9WN39*PLUS, glutamine synthetase #2: Chemical | ChemComp-MN / #3: Chemical | ChemComp-AMP / #4: Chemical | ChemComp-CIT / #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.89 Å3/Da / Density % sol: 56.98 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: PEG 4000, sodium citrate, sodium chloride, manganese chloride, imidazole buffer, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Jul 1, 1997 |
Radiation | Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.978 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→20 Å / Num. all: 566370 / Num. obs: 566370 / % possible obs: 99.6 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 4.6 % / Biso Wilson estimate: 33.1 Å2 / Rmerge(I) obs: 0.075 / Net I/σ(I): 4.5 |
Reflection shell | Resolution: 2.4→2.53 Å / Redundancy: 3.6 % / Rmerge(I) obs: 0.075 / Num. unique all: 80442 / % possible all: 98.8 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1F52 Resolution: 2.4→20 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber Details: THE CRYSTAL PACKING WAS SOLVED USING MOLECULAR REPLACEMENT TECHNIQUES USING A DODECAMER MODEL FROM SALMONELLA TYPHIMURIUM GS AS A PROBE. THE MODEL WAS SUBSEQUENTLY REDUCED TO ONE SUBUNIT ...Details: THE CRYSTAL PACKING WAS SOLVED USING MOLECULAR REPLACEMENT TECHNIQUES USING A DODECAMER MODEL FROM SALMONELLA TYPHIMURIUM GS AS A PROBE. THE MODEL WAS SUBSEQUENTLY REDUCED TO ONE SUBUNIT WITH 24-FOLD NCS-SYMMETRICAL CONSTRAINTS IMPOSED. THE SUBUNIT WAS REFINED WITH STRICT 24-FOLD NCS-AVERAGING CONSTRAINTS AND THEN USED TO REGENERATE THE ENTIRE ASYMMETRIC UNIT. AS JUSTIFIED BY LOWER R-VALUES, THE FOLLOWING RESIDUES WERE COMPLETELY RELEASED AT THE END OF THE REFINEMENT IN ORDER ACCOMMODATE CRYSTAL CONTACTS: RESIDUES 385,98,602,11,7,40,3,292.
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.4→20 Å
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Refine LS restraints |
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Xplor file | Serial no: 1 / Param file: PARHCSDX.PRO / Topol file: TOPHCSDX.PRO |