+Open data
-Basic information
Entry | Database: PDB / ID: 1bco | ||||||
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Title | BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN | ||||||
Components | BACTERIOPHAGE MU TRANSPOSASE | ||||||
Keywords | TRANSPOSASE / POLYNUCLEOTIDYL TRANSFERASE / DNA BINDING / ENDONUCLEASE / INTEGRASE | ||||||
Function / homology | Function and homology information Ligases; Forming phosphoric-ester bonds / Hydrolases; Acting on ester bonds; Endodeoxyribonucleases producing 3'-phosphomonoesters / double-stranded DNA endonuclease activity / latency-replication decision / transposase activity / DNA transposition / viral DNA genome replication / ligase activity / DNA integration / DNA replication ...Ligases; Forming phosphoric-ester bonds / Hydrolases; Acting on ester bonds; Endodeoxyribonucleases producing 3'-phosphomonoesters / double-stranded DNA endonuclease activity / latency-replication decision / transposase activity / DNA transposition / viral DNA genome replication / ligase activity / DNA integration / DNA replication / host cell cytoplasm / DNA repair / DNA binding / metal ion binding Similarity search - Function | ||||||
Biological species | Enterobacteria phage Mu (virus) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.4 Å | ||||||
Authors | Rice, P.A. / Mizuuchi, K. | ||||||
Citation | Journal: Cell(Cambridge,Mass.) / Year: 1995 Title: Structure of the bacteriophage Mu transposase core: a common structural motif for DNA transposition and retroviral integration. Authors: Rice, P. / Mizuuchi, K. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1bco.cif.gz | 88 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1bco.ent.gz | 67.3 KB | Display | PDB format |
PDBx/mmJSON format | 1bco.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/bc/1bco ftp://data.pdbj.org/pub/pdb/validation_reports/bc/1bco | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 36888.078 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterobacteria phage Mu (virus) / Genus: Mu-like viruses / Strain: WILD TYPE / Gene: MUA (AMINO ACIDS 248-574) / Plasmid: PMK602 / Gene (production host): MUA (AMINO ACIDS 248-574) / Production host: Escherichia coli (E. coli) / Strain (production host): T7 / References: UniProt: P07636 |
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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: 2.47 Å3/Da / Density % sol: 50.19 % | ||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.54 |
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Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Oct 11, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→20 Å / Num. obs: 13930 / % possible obs: 95.7 % / Observed criterion σ(I): -3 / Redundancy: 3.5 % / Rmerge(I) obs: 0.108 |
Reflection | *PLUS Highest resolution: 2.4 Å / Rmerge(I) obs: 0.108 |
-Processing
Software |
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Refinement | Resolution: 2.4→8 Å / σ(F): 1 Details: RESIDUE ARG 355 LIES IN A DISALLOWED REGION OF A RAMACHANDRAN PLOT. THIS WAS CONFIRMED IN C 2 2 21 STRUCTURE BY SIMULATED ANNEALING OMIT MAP.
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Displacement parameters | Biso mean: 16.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.4→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Version: 3.1 / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.26 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |