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Yorodumi- PDB-1dts: CRYSTAL STRUCTURE OF AN ATP DEPENDENT CARBOXYLASE, DETHIOBIOTIN S... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1dts | ||||||
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Title | CRYSTAL STRUCTURE OF AN ATP DEPENDENT CARBOXYLASE, DETHIOBIOTIN SYNTHASE, AT 1.65 ANGSTROMS RESOLUTION | ||||||
Components | DETHIOBIOTIN SYNTHETASE | ||||||
Keywords | CYCLO-LIGASE | ||||||
Function / homology | Function and homology information dethiobiotin synthase / dethiobiotin synthase activity / biotin biosynthetic process / magnesium ion binding / protein homodimerization activity / ATP binding / cytosol Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.65 Å | ||||||
Authors | Huang, W. / Lindqvist, Y. / Schneider, G. | ||||||
Citation | Journal: Structure / Year: 1994 Title: Crystal structure of an ATP-dependent carboxylase, dethiobiotin synthetase, at 1.65 A resolution. Authors: Huang, W. / Lindqvist, Y. / Schneider, G. / Gibson, K.J. / Flint, D. / Lorimer, G. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1dts.cif.gz | 57.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1dts.ent.gz | 41.5 KB | Display | PDB format |
PDBx/mmJSON format | 1dts.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1dts_validation.pdf.gz | 363 KB | Display | wwPDB validaton report |
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Full document | 1dts_full_validation.pdf.gz | 364.3 KB | Display | |
Data in XML | 1dts_validation.xml.gz | 6 KB | Display | |
Data in CIF | 1dts_validation.cif.gz | 9.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/dt/1dts ftp://data.pdbj.org/pub/pdb/validation_reports/dt/1dts | HTTPS FTP |
-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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Atom site foot note | 1: HOH 489 IS POSITIONED ON THE TWO-FOLD AXIS. | ||||||||
Components on special symmetry positions |
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-Components
#1: Protein | Mass: 23705.053 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P13000, dethiobiotin synthase |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.24 Å3/Da / Density % sol: 45.14 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 20 ℃ / pH: 6.5 / 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: 1.65 Å / Num. obs: 21608 / % possible obs: 84 % / Num. measured all: 34422 / Rmerge(I) obs: 0.076 |
-Processing
Software |
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Refinement | Resolution: 1.65→5.5 Å / σ(F): 1
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Refinement step | Cycle: LAST / Resolution: 1.65→5.5 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 2.8 |