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Open data
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Basic information
Entry | Database: PDB / ID: 6rmn | ||||||
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Title | DNA mismatch repair proteins MLH1 and MLH3 | ||||||
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![]() | RECOMBINATION / RESOLVASE / MMR / DNA REPAIR / MEIOSIS | ||||||
Function / homology | ![]() meiotic heteroduplex formation / MutLbeta complex / MutLgamma complex / MutLalpha complex / mismatch repair complex / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / meiotic mismatch repair / mismatched DNA binding / reciprocal meiotic recombination / ATP-dependent DNA damage sensor activity ...meiotic heteroduplex formation / MutLbeta complex / MutLgamma complex / MutLalpha complex / mismatch repair complex / Mismatch repair (MMR) directed by MSH2:MSH6 (MutSalpha) / meiotic mismatch repair / mismatched DNA binding / reciprocal meiotic recombination / ATP-dependent DNA damage sensor activity / mismatch repair / ATP hydrolysis activity / mitochondrion / ATP binding / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Dai, J. / Chervy, P. / Legrand, P. / Ropars, V. / Charbonnier, J.B. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Molecular basis of the dual role of the Mlh1-Mlh3 endonuclease in MMR and in meiotic crossover formation. Authors: Dai, J. / Sanchez, A. / Adam, C. / Ranjha, L. / Reginato, G. / Chervy, P. / Tellier-Lebegue, C. / Andreani, J. / Guerois, R. / Ropars, V. / Le Du, M.H. / Maloisel, L. / Martini, E. / ...Authors: Dai, J. / Sanchez, A. / Adam, C. / Ranjha, L. / Reginato, G. / Chervy, P. / Tellier-Lebegue, C. / Andreani, J. / Guerois, R. / Ropars, V. / Le Du, M.H. / Maloisel, L. / Martini, E. / Legrand, P. / Thureau, A. / Cejka, P. / Borde, V. / Charbonnier, J.B. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 219.8 KB | Display | ![]() |
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PDB format | ![]() | 174.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 517 KB | Display | ![]() |
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Full document | ![]() | 520.1 KB | Display | |
Data in XML | ![]() | 19.2 KB | Display | |
Data in CIF | ![]() | 27.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6shxC ![]() 6snsC ![]() 6snvC ![]() 4e4wS 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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1 |
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Unit cell |
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Components
#1: Protein | Mass: 30764.279 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Saccharomyces cerevisiae S288C / Gene: MLH1, PMS2, YMR167W, YM8520.16 / Variant: ATCC 204508 / S288c / Production host: ![]() ![]() | ||
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#2: Protein | Mass: 27638.000 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: The six X letters correspond to a proposed loop not assigned in sequence (unk in pdb for unknown) Source: (gene. exp.) Saccharomyces cerevisiae S288C / Gene: MLH3, YPL164C, P2550 / Variant: ATCC 204508 / S288c / Production host: ![]() ![]() | ||
#3: Chemical | #4: Water | ChemComp-HOH / | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.12 Å3/Da / Density % sol: 60.63 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 6 Details: 10% PEG4000, 200 mM imidazole-malate, pH6 and 10 mM MgCl2 |
-Data collection
Diffraction | Mean temperature: 163 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Jun 13, 2015 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97857 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→48.4 Å / Num. obs: 33362 / % possible obs: 98.7 % / Redundancy: 13 % / Biso Wilson estimate: 51.47 Å2 / Rmerge(I) obs: 0.1 / Rpim(I) all: 0.029 / Rrim(I) all: 0.104 / Net I/σ(I): 12.8 |
Reflection shell | Resolution: 2.2→2.25 Å / Redundancy: 11.3 % / Num. unique obs: 2168 / Rpim(I) all: 0.42 / % possible all: 87.4 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 4E4W Resolution: 2.2→38.14 Å / Cor.coef. Fo:Fc: 0.943 / Cor.coef. Fo:Fc free: 0.942 / SU R Cruickshank DPI: 0.381 / Cross valid method: THROUGHOUT / σ(F): 0 / SU R Blow DPI: 0.382 / SU Rfree Blow DPI: 0.234 / SU Rfree Cruickshank DPI: 0.236
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Displacement parameters | Biso mean: 69.09 Å2
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Refine analyze | Luzzati coordinate error obs: 0.32 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→38.14 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.2→2.33 Å / Total num. of bins used: 50
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Refinement TLS params. | Method: refined / Origin x: 28.7898 Å / Origin y: 16.2721 Å / Origin z: 20.6711 Å
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Refinement TLS group | Selection details: { *|* } |