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Yorodumi- PDB-1kan: MOLECULAR STRUCTURE OF KANAMYCIN NUCLEOTIDYLTRANSFERASE DETERMINE... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1kan | ||||||
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Title | MOLECULAR STRUCTURE OF KANAMYCIN NUCLEOTIDYLTRANSFERASE DETERMINED TO 3.0-ANGSTROMS RESOLUTION | ||||||
Components | KANAMYCIN NUCLEOTIDYLTRANSFERASE | ||||||
Keywords | NUCLEOTIDYLTRANSFERASE | ||||||
Function / homology | Kanamycin nucleotidyltransferase, C-terminal / KNTase C-terminal domain / nucleotidyltransferase activity / Nucleotidyltransferase superfamily / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / response to antibiotic / Kanamycin nucleotidyltransferase Function and homology information | ||||||
Biological species | Staphylococcus aureus (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 3 Å | ||||||
Authors | Holden, H.M. / Rayment, I. / Sakon, J. | ||||||
Citation | Journal: Biochemistry / Year: 1993 Title: Molecular structure of kanamycin nucleotidyltransferase determined to 3.0-A resolution. Authors: Sakon, J. / Liao, H.H. / Kanikula, A.M. / Benning, M.M. / Rayment, I. / Holden, H.M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1kan.cif.gz | 27 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1kan.ent.gz | 14.5 KB | Display | PDB format |
PDBx/mmJSON format | 1kan.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ka/1kan ftp://data.pdbj.org/pub/pdb/validation_reports/ka/1kan | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 28901.689 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Staphylococcus aureus (bacteria) References: UniProt: P05057, Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.95 Å3/Da / Density % sol: 58.31 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 8 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 3 Å / Lowest resolution: 9999 Å / Num. obs: 13914 / % possible obs: 95 % / Num. measured all: 70244 / Rmerge(I) obs: 0.075 |
Reflection shell | *PLUS Highest resolution: 3 Å / Lowest resolution: 3.21 Å / % possible obs: 2243 % / Num. possible: 96 / Num. unique obs: 3586 / Rmerge(I) obs: 0.209 |
-Processing
Software | Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
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Refinement | Rfactor obs: 0.189 / Highest resolution: 3 Å | ||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 3 Å
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Refine LS restraints |
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Software | *PLUS Name: TNT / Classification: refinement | ||||||||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 30 Å / Rfactor obs: 0.189 | ||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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