+Open data
-Basic information
Entry | Database: PDB / ID: 2z11 | ||||||
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Title | Crystal structure of putative acetyltransferase | ||||||
Components | Ribosomal-protein-alanine acetyltransferase | ||||||
Keywords | TRANSFERASE / alpha/beta protein / Acyltransferase / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | ||||||
Function / homology | Function and homology information ribosomal-protein-alanine N-acetyltransferase / acyltransferase activity, transferring groups other than amino-acyl groups Similarity search - Function | ||||||
Biological species | Thermus thermophilus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SAD / Resolution: 2.15 Å | ||||||
Authors | Murayama, K. / Kato-Murayama, M. / Terada, T. / Kuramitsu, S. / Shirouzu, M. / Yokoyama, S. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | ||||||
Citation | Journal: To be Published Title: Crystal structure of putative acetyltransferase Authors: Murayama, K. / Kato-Murayama, M. / Terada, T. / Shirouzu, M. / Yokoyama, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2z11.cif.gz | 49.1 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2z11.ent.gz | 38.2 KB | Display | PDB format |
PDBx/mmJSON format | 2z11.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/z1/2z11 ftp://data.pdbj.org/pub/pdb/validation_reports/z1/2z11 | HTTPS FTP |
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-Related structure data
Similar structure data | |
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Other databases |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 22288.467 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermus thermophilus (bacteria) / Strain: HB27 / Plasmid: pET11a / Production host: Escherichia coli (E. coli) References: UniProt: Q72HN8, ribosomal-protein-alanine N-acetyltransferase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.23 Å3/Da / Density % sol: 61.93 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: 0.15M ammonium acetate, 0.1M bis-tris(5.5), 28% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU FR-E+ SUPERBRIGHT / Wavelength: 2.29 Å |
Detector | Type: RIGAKU RAXIS VII / Detector: IMAGE PLATE / Date: Oct 28, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 2.29 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→50 Å / Num. obs: 16175 / % possible obs: 99.8 % / Observed criterion σ(I): -3 / Redundancy: 17.6 % / Biso Wilson estimate: 31.1 Å2 / Rsym value: 0.076 / Net I/σ(I): 35 |
Reflection shell | Resolution: 2.15→2.23 Å / Redundancy: 10.3 % / Mean I/σ(I) obs: 9.6 / Rsym value: 0.262 / % possible all: 98.4 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 2.15→33.4 Å / Rfactor Rfree error: 0.006 / Data cutoff high absF: 1130194.84 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 53.1568 Å2 / ksol: 0.358955 e/Å3 | ||||||||||||||||||||
Displacement parameters | Biso mean: 32.8 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.15→33.4 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.15→2.28 Å / Rfactor Rfree error: 0.019 / Total num. of bins used: 6
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Xplor file |
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