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Open data
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Basic information
Entry | Database: PDB / ID: 2hut | ||||||
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Title | Crystal structure of PH0725 from Pyrococcus horikoshii OT3 | ||||||
![]() | Probable diphthine synthase | ||||||
![]() | TRANSFERASE / Pyrococcus horikoshii OT3 / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | ![]() diphthine synthase / diphthine synthase activity / protein histidyl modification to diphthamide / methylation Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Sugahara, M. / Saraboji, K. / Malathy sony, S.M. / Ponnuswamy, M.N. / Kumarevel, T.S. / Kunishima, N. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
![]() | ![]() Title: Crystal structure of PH0725 from Pyrococcus horikoshii OT3 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 | ![]() | 119.8 KB | Display | ![]() |
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PDB format | ![]() | 92.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 779 KB | Display | ![]() |
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Full document | ![]() | 786.6 KB | Display | |
Data in XML | ![]() | 22.9 KB | Display | |
Data in CIF | ![]() | 32.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2e8hC ![]() 2hr8C ![]() 2huqC ![]() 2huvC ![]() 2huxC ![]() 2owfC ![]() 2owgC ![]() 2owkC ![]() 2owuC ![]() 2owvC ![]() 2p2xC ![]() 2p5cC ![]() 2p5fC ![]() 2p6dC ![]() 2p6iC ![]() 2p6kC ![]() 2p6lC ![]() 2p9dC ![]() 2pb4C ![]() 2pb5C ![]() 2pb6C ![]() 2pcaC ![]() 2pcgC ![]() 2pchC ![]() 2pciC ![]() 2pckC ![]() 2pcmC ![]() 1vceS 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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Unit cell |
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Details | The biological assembly is a dimer in the asymmetric unit |
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Components
#1: Protein | Mass: 29631.404 Da / Num. of mol.: 2 / Mutation: L72M Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | ChemComp-SAH / | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.25 Å3/Da / Density % sol: 62.13 % |
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Crystal grow | Temperature: 295 K / Method: microbatch / pH: 7 Details: Sodium malonate, MES, pH 7.0, microbatch, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS VII / Detector: IMAGE PLATE / Date: Nov 30, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→15 Å / Num. all: 31141 / Num. obs: 31141 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 10.6 % / Biso Wilson estimate: 53.76 Å2 / Rmerge(I) obs: 0.062 / Rsym value: 0.059 / Net I/σ(I): 13 |
Reflection shell | Resolution: 2.4→2.49 Å / Redundancy: 9.6 % / Rmerge(I) obs: 0.582 / Mean I/σ(I) obs: 4.3 / Num. unique all: 3036 / Rsym value: 0.555 / % possible all: 99.6 |
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Processing
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Refinement | Method to determine structure: DIFFERENCE FOURIER Starting model: PDB ENTRY 1VCE Resolution: 2.4→14.99 Å / Isotropic thermal model: Anisotrop / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 46.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.4→14.99 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.4→2.49 Å / Rfactor Rfree error: 0.028
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