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- PDB-1bcm: BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN WITH 2 MONOMERS PER ASYM... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1bcm | ||||||
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Title | BACTERIOPHAGE MU TRANSPOSASE CORE DOMAIN WITH 2 MONOMERS PER ASYMMETRIC UNIT | ||||||
![]() | BACTERIOPHAGE MU TRANSPOSASE | ||||||
![]() | TRANSPOSASE / POLYNUCLEOTIDYL TRANSFERASE / DNA BINDING / ENDONUCLEASE / INTEGRASE | ||||||
Function / homology | ![]() 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 | ![]() | ||||||
Method | ![]() | ||||||
![]() | Rice, P.A. / Mizuuchi, K. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 147.7 KB | Display | ![]() |
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PDB format | ![]() | 117.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.6177, -0.0594, -0.7841), Vector: Details | MTRIX THE TRANSFORMATIONS PRESENTED ON MTRIX RECORDS BELOW DESCRIBE NON-CRYSTALLOGRAPHIC RELATIONSHIPS AMONG THE VARIOUS DOMAINS IN THIS ENTRY. APPLYING THE APPROPRIATE MTRIX TRANSFORMATION TO THE RESIDUES LISTED FIRST WILL YIELD APPROXIMATE COORDINATES FOR THE RESIDUES LISTED SECOND. APPLIED TO TRANSFORMED TO MTRIX RESIDUES RESIDUES RMSD M1 B 258 .. B 560 A 258 .. A 560 0.593 THIS REPRESENTS A NON-CRYSTALLOGRAPHIC TWO-FOLD AXIS. | |
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Components
#1: Protein | Mass: 36888.078 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.79 Å3/Da / Density % sol: 55.95 % | ||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS 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 / Detector: IMAGE PLATE / Date: Aug 27, 1994 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→20 Å / Num. obs: 21089 / % possible obs: 92.5 % / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Rmerge(I) obs: 0.095 |
Reflection | *PLUS Highest resolution: 2.7 Å / Rmerge(I) obs: 0.095 |
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Processing
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Refinement | Resolution: 2.8→8 Å / σ(F): 1 Details: RESIDUES ARG A 355 AND ARG B 355 LIE IN A DISALLOWED REGION OF A RAMACHANDRAN PLOT. THIS WAS CONFIRMED IN THE C 2 2 21 STRUCTURE BY SIMULATED ANNEALING OMIT MAP.
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Displacement parameters | Biso mean: 20.7 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS Highest resolution: 2.8 Å / Lowest resolution: 2.92 Å |