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- PDB-6ac8: Crystal structure of Mycobacterium smegmatis Mfd at 2.75 A resolution -
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Open data
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Basic information
Entry | Database: PDB / ID: 6ac8 | ||||||
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Title | Crystal structure of Mycobacterium smegmatis Mfd at 2.75 A resolution | ||||||
![]() | Mycobacterium smegmatis Mfd | ||||||
![]() | HYDROLASE / Transcription repair coupling factor / Mfd / Transcription regulation / Transcription Coupled Nucleotide Excision Repair. | ||||||
Function / homology | ![]() transcription-coupled nucleotide-excision repair, DNA damage recognition / DNA helicase activity / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / damaged DNA binding / hydrolase activity / regulation of DNA-templated transcription / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Putta, S. / Fox, G.C. / Walsh, M.A. / Rao, D.N. / Nagaraja, V. / Natesh, R. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for nucleotide-mediated remodelling mechanism of Mycobacterium Mfd Authors: Putta, S. / Prabha, S. / Bhat, V. / Fox, G.C. / Walsh, M.A. / Rao, D.N. / Nagaraja, V. / Natesh, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 450.4 KB | Display | ![]() |
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PDB format | ![]() | 353.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 472.6 KB | Display | ![]() |
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Full document | ![]() | 506.3 KB | Display | |
Data in XML | ![]() | 79.2 KB | Display | |
Data in CIF | ![]() | 106.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 9614C ![]() 6ac6SC ![]() 6acaC ![]() 6acxC 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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2 | ![]()
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3 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 133438.484 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: Amplified from Mycobacterium smegmatis genomic DNA Source: (gene. exp.) ![]() Strain: MC2 155 / Gene: mfd / Plasmid: pETMsMfd / Details (production host): Amplied MsMfd cloned into pET28a / Production host: ![]() ![]() References: UniProt: I7G7M2, UniProt: A0R3C5*PLUS, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement #2: Chemical | ChemComp-SO4 / #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.79 Å3/Da / Density % sol: 55.98 % / Description: Rhomboid |
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Crystal grow | Temperature: 295 K / Method: vapor diffusion, hanging drop / pH: 7.2 Details: 100mM HEPES sodium pH 7.2, 0.2M Na2So4, 20% PEG3350 PH range: 7.2-7.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M / Detector: PIXEL / Date: Dec 11, 2015 |
Radiation | Monochromator: double crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9763 Å / Relative weight: 1 |
Reflection | Resolution: 2.75→40.59 Å / Num. obs: 76641 / % possible obs: 99.5 % / Observed criterion σ(I): 1.6 / Redundancy: 4.5 % / Biso Wilson estimate: 73.092 Å2 / CC1/2: 0.994 / Rmerge(I) obs: 0.076 / Rpim(I) all: 0.041 / Rrim(I) all: 0.091 / Rsym value: 0.08 / Net I/σ(I): 9 |
Reflection shell | Resolution: 2.75→2.81 Å / Redundancy: 4.3 % / Rmerge(I) obs: 0.826 / Mean I/σ(I) obs: 1.6 / Num. unique obs: 4531 / CC1/2: 0.456 / Rpim(I) all: 0.633 / Rrim(I) all: 1.041 / Rsym value: 0.914 / % possible all: 99.7 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 6AC6 Resolution: 2.75→40.507 Å / SU ML: 0.46 / Cross valid method: FREE R-VALUE / σ(F): 1.34 / Phase error: 29.22 / Details: Phenix refinement
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Refinement step | Cycle: LAST / Resolution: 2.75→40.507 Å
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Refine LS restraints |
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LS refinement shell |
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