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- PDB-2cu2: Crystal structure of mannose-1-phosphate geranyltransferase from ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2cu2 | ||||||
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Title | Crystal structure of mannose-1-phosphate geranyltransferase from Thermus thermophilus HB8 | ||||||
![]() | putative mannose-1-phosphate guanylyl transferase | ||||||
![]() | TRANSFERASE / mannose-1-phosphate geranyltransferase / Thermus thermophilus HB8 / Structural Genomics / RIKEN Structural Genomics/Proteomics Initiative / RSGI / NPPSFA / National Project on Protein Structural and Functional Analyses | ||||||
Function / homology | ![]() biosynthetic process / isomerase activity / nucleotidyltransferase activity Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Sugahara, M. / Kunishima, N. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
![]() | ![]() Title: Crystal structure of mannose-1-phosphate geranyltransferase from Thermus thermophilus HB8 Authors: Sugahara, M. / Kunishima, N. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 82.1 KB | Display | ![]() |
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PDB format | ![]() | 61.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 438.2 KB | Display | ![]() |
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Full document | ![]() | 444.1 KB | Display | |
Data in XML | ![]() | 16.9 KB | Display | |
Data in CIF | ![]() | 24.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | |
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Other databases |
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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 on special symmetry positions |
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Details | The biological assembly is a dimer in the asymmetric unit by the operations: -x+1, y, -z+1. |
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Components
#1: Protein | Mass: 37487.867 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: Q5SHI0, mannose-1-phosphate guanylyltransferase | ||
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#2: Chemical | #3: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.1 Å3/Da / Density % sol: 59.7 % |
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Crystal grow | Temperature: 295 K / Method: microbatch / pH: 8.5 Details: lithium sulphate, pH 8.5, microbatch , temperature 295K |
-Data collection
Diffraction |
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Diffraction source |
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Detector |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||
Radiation wavelength |
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Reflection | Resolution: 2.2→40 Å / Num. all: 23487 / Num. obs: 23487 / % possible obs: 99.9 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 8 % / Biso Wilson estimate: 39.749 Å2 / Rmerge(I) obs: 0.07 / Rsym value: 0.066 / Net I/σ(I): 10.1 | |||||||||||||||
Reflection shell | Resolution: 2.2→2.28 Å / Redundancy: 8.1 % / Rmerge(I) obs: 0.62 / Mean I/σ(I) obs: 3.8 / Num. unique all: 2307 / Rsym value: 0.58 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 41.1 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.2→37.98 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.28 Å / Rfactor Rfree error: 0.028
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