+Open data
-Basic information
Entry | Database: PDB / ID: 2reb | ||||||
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Title | THE STRUCTURE OF THE E. COLI RECA PROTEIN MONOMER AND POLYMER | ||||||
Components | REC A | ||||||
Keywords | DNA BINDING PROTEIN / SELF-CLEAVAGE STIMULATION / HOMOLOGOUS RECOMBINATION | ||||||
Function / homology | Function and homology information DNA polymerase V complex / homologous recombination / recombinational repair / ATP-dependent DNA damage sensor activity / response to ionizing radiation / SOS response / ATP-dependent activity, acting on DNA / translesion synthesis / cell motility / single-stranded DNA binding ...DNA polymerase V complex / homologous recombination / recombinational repair / ATP-dependent DNA damage sensor activity / response to ionizing radiation / SOS response / ATP-dependent activity, acting on DNA / translesion synthesis / cell motility / single-stranded DNA binding / DNA-binding transcription factor binding / DNA recombination / damaged DNA binding / DNA damage response / ATP hydrolysis activity / ATP binding / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Story, R.M. / Steitz, T.A. | ||||||
Citation | Journal: Nature / Year: 1992 Title: The structure of the E. coli recA protein monomer and polymer. Authors: Story, R.M. / Weber, I.T. / Steitz, T.A. #1: Journal: Nature / Year: 1992 Title: Structure of the Reca Protein-Adp Complex Authors: Story, R.M. / Steitz, T.A. #2: Journal: Nature / Year: 1992 Title: The Structure of the E. Coli Reca Protein Monomer and Polymer: Erratum Authors: Story, R.M. / Weber, I.T. / Steitz, T.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2reb.cif.gz | 70.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2reb.ent.gz | 52.7 KB | Display | PDB format |
PDBx/mmJSON format | 2reb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/re/2reb ftp://data.pdbj.org/pub/pdb/validation_reports/re/2reb | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Atom site foot note | 1: THE PEPTIDE BOND BETWEEN ASP 144 AND SER 145 HAS BEEN BUILT IN THE CIS CONFORMATION. |
-Components
#1: Protein | Mass: 37885.086 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / References: UniProt: P0A7G6 |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.3 Å3/Da / Density % sol: 62.76 % | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 5.4 / Method: microdialysis | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | *PLUS Highest resolution: 2.3 Å / % possible obs: 92 % / Rmerge(I) obs: 0.055 |
-Processing
Software |
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Refinement | Rfactor Rwork: 0.21 / Rfactor obs: 0.21 / Highest resolution: 2.3 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Highest resolution: 2.3 Å
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Refine LS restraints |
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