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- PDB-2zgw: Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horiko... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2zgw | |||||||||
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Title | Crystal Structure Of Biotin Protein Ligase From Pyrococcus Horikoshii Complexed with Adenosine and Biotin, Mutations R48A and K111A | |||||||||
![]() | biotin--[acetyl-CoA-carboxylase] ligase | |||||||||
![]() | LIGASE / Biotin Biosynthesis / Dimer / Structural Genomics / NPPSFA / National Project on Protein Structural and Functional Analyses / RIKEN Structural Genomics/Proteomics Initiative / RSGI | |||||||||
Function / homology | ![]() biotin--[biotin carboxyl-carrier protein] ligase activity / protein modification process / ATP binding / metal ion binding / cytoplasm Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Bagautdinov, B. / Matsuura, Y. / Bagautdinova, S. / Kunishima, N. / RIKEN Structural Genomics/Proteomics Initiative (RSGI) | |||||||||
![]() | ![]() Title: Protein biotinylation visualized by a complex structure of biotin protein ligase with a substrate Authors: Bagautdinov, B. / Matsuura, Y. / Bagautdinova, S. / 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 | ![]() | 118.9 KB | Display | ![]() |
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PDB format | ![]() | 89.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 26 KB | Display | |
Data in CIF | ![]() | 39.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1x01C ![]() 2d5dC ![]() 2dxuC ![]() 2dzcC ![]() 2e41C ![]() 2e64C ![]() 2ejfC ![]() 2ejgC ![]() 2evbC ![]() 1wqwS S: Starting model for refinement C: citing same article ( |
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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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Components
#1: Protein | Mass: 25959.305 Da / Num. of mol.: 2 / Mutation: R48A, K111A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 43 % |
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Crystal grow | Temperature: 295 K / Method: microbatch / pH: 5.2 Details: PEG20K, Acetate, NaOH, ATP, Biotin, pH 5.2, microbatch, temperature 295K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Oct 3, 2006 / Details: mirrors |
Radiation | Monochromator: GRAPHITE / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→41.44 Å / Num. all: 70522 / Num. obs: 69128 / % possible obs: 98 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.6 % / Biso Wilson estimate: 16.09 Å2 / Rmerge(I) obs: 0.042 / Rsym value: 0.032 / Net I/σ(I): 12.8 |
Reflection shell | Resolution: 1.5→1.55 Å / Redundancy: 3.3 % / Rmerge(I) obs: 0.274 / Mean I/σ(I) obs: 2.1 / Num. unique all: 6367 / Rsym value: 0.239 / % possible all: 95.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1wqw Resolution: 1.5→37.25 Å / Isotropic thermal model: Overall / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters | Biso mean: 19.7 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 1.5→37.25 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.5→1.55 Å / Rfactor Rfree error: 0.015
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