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Open data
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Basic information
Entry | Database: PDB / ID: 5fos | ||||||
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Title | HUMANISED MONOMERIC RADA IN COMPLEX WITH OLIGOMERISATION PEPTIDE | ||||||
![]() | (DNA REPAIR AND RECOMBINATION PROTEIN RADA) x 2 | ||||||
![]() | HYDROLASE / FXXA MOTIF / RECOMBINASE | ||||||
Function / homology | ![]() DNA recombinase assembly / mitotic recombination / DNA strand invasion / DNA strand exchange activity / ATP-dependent DNA damage sensor activity / single-stranded DNA binding / double-stranded DNA binding / damaged DNA binding / ATP hydrolysis activity / ATP binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Sharpe, T. / Moschetti, T. / Fischer, G. / Marsh, M. / Blundell, T.L. / Abell, C. / Hyvonen, M. | ||||||
![]() | ![]() Title: Engineering Archeal Surrogate Systems for the Development of Protein-Protein Interaction Inhibitors against Human RAD51. Authors: Moschetti, T. / Sharpe, T. / Fischer, G. / Marsh, M.E. / Ng, H.K. / Morgan, M. / Scott, D.E. / Blundell, T.L. / R Venkitaraman, A. / Skidmore, J. / Abell, C. / Hyvonen, M. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 158.6 KB | Display | ![]() |
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PDB format | ![]() | 127.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 455 KB | Display | ![]() |
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Full document | ![]() | 456.8 KB | Display | |
Data in XML | ![]() | 14.5 KB | Display | |
Data in CIF | ![]() | 21.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5j4hC ![]() 5j4kC ![]() 5j4lC ![]() 5jecC ![]() 5jedC ![]() 5jeeC ![]() 5kddC ![]() 5l8vC ![]() 5lb2C ![]() 5lb4C ![]() 5lbiC ![]() 1pznS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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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: 25502.150 Da / Num. of mol.: 1 / Fragment: ATPASE, UNP RESIDUES 108-349 / Mutation: YES Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: O74036, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement | ||||
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#2: Protein/peptide | Mass: 1915.245 Da / Num. of mol.: 1 / Fragment: OLIGOMERISATION PEPTIDE, UNP RESIDUES 93-108 / Source method: obtained synthetically / Source: (synth.) ![]() ![]() References: UniProt: O74036, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement | ||||
#3: Chemical | ChemComp-PO4 / | ||||
#4: Chemical | ChemComp-GOL / #5: Water | ChemComp-HOH / | Sequence details | MUTATIONS I169M, Y201A, V202Y, K221M AND REPLACEMENT OF LOOP 287-300 BY AN N. MUTATIONS I169M, ...MUTATIONS I169M, Y201A, V202Y, K221M AND REPLACEMEN | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.16 Å3/Da / Density % sol: 43.2 % / Description: NONE |
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Crystal grow | pH: 6.2 / Details: 8% PEG-1000, 100 MM NAK PHOSPHATE, PH 6.2 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Jul 31, 2008 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 1.35→36.95 Å / Num. obs: 47394 / % possible obs: 96.3 % / Observed criterion σ(I): 2 / Redundancy: 4.9 % / Biso Wilson estimate: 18.5 Å2 / Rmerge(I) obs: 0.06 / Net I/σ(I): 16.33 |
Reflection shell | Resolution: 1.35→1.43 Å / Redundancy: 4.77 % / Rmerge(I) obs: 0.55 / Mean I/σ(I) obs: 2.65 / % possible all: 98.6 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1PZN Resolution: 1.35→36.949 Å / SU ML: 0.12 / σ(F): 1.99 / Phase error: 15.99 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 18.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.35→36.949 Å
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Refine LS restraints |
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LS refinement shell |
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