|Entry||Database: PDB / ID: 2odw|
|Keywords||RECOMBINATION / DNA-REPAIR / SOS RESPONCE|
|Function / homology|
Function and homology information
SOS response / ATP-dependent activity, acting on DNA / single-stranded DNA binding / DNA recombination / damaged DNA binding / DNA repair / ATP binding / cytoplasm
Similarity search - Function
RecA protein, C-terminal domain / Rec A Protein; domain 2 / recA signature. / DNA recombination and repair protein RecA, C-terminal / DNA recombination/repair protein RecA, conserved site / recA bacterial DNA recombination protein / DNA recombination and repair protein RecA / RecA family profile 2. / DNA recombination and repair protein RecA, monomer-monomer interface / RecA family profile 1. ...RecA protein, C-terminal domain / Rec A Protein; domain 2 / recA signature. / DNA recombination and repair protein RecA, C-terminal / DNA recombination/repair protein RecA, conserved site / recA bacterial DNA recombination protein / DNA recombination and repair protein RecA / RecA family profile 2. / DNA recombination and repair protein RecA, monomer-monomer interface / RecA family profile 1. / DNA recombination and repair protein RecA-like, ATP-binding domain / P-loop containing nucleotide triphosphate hydrolases / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase / Rossmann fold / 2-Layer Sandwich / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / Protein RecA
Similarity search - Component
|Biological species||Mycobacterium smegmatis (bacteria)|
|Method||X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 3.3 Å|
|Authors||Krishna, R. / Rajan Prabu, J. / Manjunath, G.P. / Datta, S. / Chandra, N.R. / Muniyappa, K. / Vijayan, M.|
Journal: J.Mol.Biol. / Year: 2007
Title: Snapshots of RecA protein involving movement of the C-domain and different conformations of the DNA-binding loops: crystallographic and comparative analysis of 11 structures of Mycobacterium smegmatis RecA
Authors: Krishna, R. / Prabu, J.R. / Manjunath, G.P. / Datta, S. / Chandra, N.R. / Muniyappa, K. / Vijayan, M.
#1: Journal: Nucleic Acids Res. / Year: 2000
Title: Crystal structures of Mycobacterium tuberculosis RecA and its complex with ADP-AlF(4): implications for decreased ATPase activity and molecular aggregation
Authors: Datta, S. / Prabu, M.M. / Vaze, M.B. / Ganesh, N. / Chandra, N.R. / Muniyappa, K. / Vijayan, M.
#2: Journal: Proteins / Year: 2003
Title: Structural studies on MtRecA-nucleotide complexes: insights into DNA and nucleotide binding and the structural signature of NTP recognition
Authors: Datta, S. / Ganesh, N. / Chandra, N.R. / Muniyappa, K. / Vijayan, M.
#3: Journal: J.Bacteriol. / Year: 2003
Title: Crystal structures of Mycobacterium smegmatis RecA and its nucleotide complexes
Authors: Datta, S. / Krishna, R. / Ganesh, N. / Chandra, N.R. / Muniyappa, K. / Vijayan, M.
|Structure viewer||Molecule: |
Downloads & links
A: Protein recA
|#1: Protein|| |
Mass: 37344.488 Da / Num. of mol.: 1
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mycobacterium smegmatis (bacteria) / Plasmid: PTHIOA / Production host: Escherichia coli (E. coli) / Strain (production host): JC10289 / References: UniProt: Q59560, EC: 188.8.131.52
|#2: Chemical|| ChemComp-AGS / |
|#3: Water|| ChemComp-HOH / |
|Experiment||Method: X-RAY DIFFRACTION / Number of used crystals: 1|
|Crystal||Density Matthews: 3.08 Å3/Da / Density % sol: 60.04 %|
|Crystal grow||Temperature: 293 K / Method: vapor diffusion, hanging drop / pH: 7.5 |
Details: Citrate Phosphate, PEG 4000, NACL, Sodium citrate, pH 7.50, VAPOR DIFFUSION, HANGING DROP, temperature 293K
|Diffraction||Mean temperature: 293 K|
|Diffraction source||Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 / Wavelength: 1.5418 Å|
|Detector||Type: MARRESEARCH / Detector: IMAGE PLATE / Date: May 13, 2003|
|Radiation||Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray|
|Radiation wavelength||Wavelength: 1.5418 Å / Relative weight: 1|
|Reflection||Resolution: 3.3→25.8 Å / Num. obs: 6712 / % possible obs: 96.8 % / Observed criterion σ(I): 0 / Redundancy: 4.9 % / Rmerge(I) obs: 0.097 / Net I/σ(I): 6.6|
|Reflection shell||Resolution: 3.3→3.42 Å / Redundancy: 4.4 % / Rmerge(I) obs: 0.45 / Mean I/σ(I) obs: 1.9 / % possible all: 97.4|
|Refinement||Method to determine structure: MOLECULAR REPLACEMENT|
Starting model: 1UBC
Resolution: 3.3→25.76 Å / Rfactor Rfree error: 0.011 / Data cutoff high absF: 145049.57 / Data cutoff low absF: 0 / Isotropic thermal model: GROUP / Cross valid method: THROUGHOUT / σ(F): 0
|Solvent computation||Solvent model: FLAT MODEL / Bsol: 40.3942 Å2 / ksol: 0.206769 e/Å3|
|Displacement parameters||Biso mean: 48.5 Å2|
|Refinement step||Cycle: LAST / Resolution: 3.3→25.76 Å|
|Refine LS restraints|
|LS refinement shell||Resolution: 3.3→3.51 Å / Rfactor Rfree error: 0.037 / Total num. of bins used: 6 |
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