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- PDB-1loo: Crystal Structure of the Mouse-Muscle Adenylosuccinate Synthetase... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1loo | ||||||
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Title | Crystal Structure of the Mouse-Muscle Adenylosuccinate Synthetase Ligated with GTP | ||||||
![]() | adenylosuccinate synthetase | ||||||
![]() | LIGASE / Purine biosynthesis / GTP-binding | ||||||
Function / homology | ![]() Purine ribonucleoside monophosphate biosynthesis / purine nucleotide metabolic process / adenylosuccinate synthase / adenylosuccinate synthase activity / aspartate metabolic process / IMP metabolic process / 'de novo' AMP biosynthetic process / AMP salvage / actin filament binding / GTPase activity ...Purine ribonucleoside monophosphate biosynthesis / purine nucleotide metabolic process / adenylosuccinate synthase / adenylosuccinate synthase activity / aspartate metabolic process / IMP metabolic process / 'de novo' AMP biosynthetic process / AMP salvage / actin filament binding / GTPase activity / GTP binding / magnesium ion binding / identical protein binding / membrane / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Iancu, C.V. / Borza, T. / Fromm, H.J. / Honzatko, R.B. | ||||||
![]() | ![]() Title: IMP, GTP, and 6-phosphoryl-IMP complexes of recombinant mouse muscle adenylosuccinate synthetase. Authors: Iancu, C.V. / Borza, T. / Fromm, H.J. / Honzatko, R.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 98.1 KB | Display | ![]() |
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PDB format | ![]() | 74.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 759.6 KB | Display | ![]() |
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Full document | ![]() | 772.6 KB | Display | |
Data in XML | ![]() | 19.5 KB | Display | |
Data in CIF | ![]() | 26.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1iweC ![]() 1lnyC ![]() 1lonC ![]() 1j4bS 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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Unit cell |
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Details | The biological assembly is a dimer. The asymmetric unit contains one monomer. The other monomer is generated by the symmetry operation: -y, -x, 1/2-z. |
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Components
#1: Protein | Mass: 50321.301 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-GTP / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.41 Å3/Da / Density % sol: 48.87 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 296 K / Method: vapor diffusion, hanging drop / pH: 7 Details: PEG 8000, magnesium acetate, pH 7, VAPOR DIFFUSION, HANGING DROP, temperature 296K | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Mar 19, 2002 / Details: osmic mirrors |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→65.9 Å / Num. all: 25715 / Num. obs: 21799 / % possible obs: 91.5 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 4.9 % / Biso Wilson estimate: 47.4 Å2 / Rmerge(I) obs: 0.04 / Net I/σ(I): 20 |
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 4 % / Rmerge(I) obs: 0.255 / Mean I/σ(I) obs: 2.3 / Num. unique all: 2124 / % possible all: 89.5 |
Reflection | *PLUS Num. obs: 25715 / % possible obs: 89.5 % / Num. measured all: 126081 / Rmerge(I) obs: 0.081 |
Reflection shell | *PLUS Lowest resolution: 2.3 Å / % possible obs: 98.5 % / Rmerge(I) obs: 0.312 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1J4B Resolution: 2.2→10 Å / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 46.9 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.2→10 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.34 Å / Rfactor Rfree error: 0.02
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Refinement | *PLUS Lowest resolution: 10 Å / Num. reflection obs: 25407 / % reflection Rfree: 10 % / Rfactor Rfree: 0.276 / Rfactor Rwork: 0.244 | |||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Rfactor Rfree: 0.382 / Rfactor Rwork: 0.338 |