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Yorodumi- PDB-1rcn: CRYSTAL STRUCTURE OF THE RIBONUCLEASE A D(APTPAPAPG) COMPLEX : DI... -
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Open data
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Basic information
| Entry | Database: PDB / ID: 1rcn | ||||||
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| Title | CRYSTAL STRUCTURE OF THE RIBONUCLEASE A D(APTPAPAPG) COMPLEX : DIRECT EVIDENCE FOR EXTENDED SUBSTRATE RECOGNITION | ||||||
Components |
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Keywords | HYDROLASE/DNA / PROTEIN-DNA COMPLEX / HYDROLASE-DNA COMPLEX | ||||||
| Function / homology | Function and homology informationpancreatic ribonuclease / ribonuclease A activity / RNA nuclease activity / nucleic acid binding / defense response to Gram-positive bacterium / lyase activity / extracellular region Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / Resolution: 2.32 Å | ||||||
Authors | Fontecilla-Camps, J.C. / De Llorens, R. / Le Du, M.H. / Cuchillo, C.M. | ||||||
Citation | Journal: J.Biol.Chem. / Year: 1994Title: Crystal structure of ribonuclease A.d(ApTpApApG) complex. Direct evidence for extended substrate recognition. Authors: Fontecilla-Camps, J.C. / de Llorens, R. / le Du, M.H. / Cuchillo, C.M. | ||||||
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1rcn.cif.gz | 39.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1rcn.ent.gz | 26.8 KB | Display | PDB format |
| PDBx/mmJSON format | 1rcn.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 1rcn_validation.pdf.gz | 371.1 KB | Display | wwPDB validaton report |
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| Full document | 1rcn_full_validation.pdf.gz | 378.6 KB | Display | |
| Data in XML | 1rcn_validation.xml.gz | 5.2 KB | Display | |
| Data in CIF | 1rcn_validation.cif.gz | 7.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/rc/1rcn ftp://data.pdbj.org/pub/pdb/validation_reports/rc/1rcn | HTTPS FTP |
-Related structure data
| 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: DNA chain | Mass: 1198.856 Da / Num. of mol.: 1 / Source method: obtained synthetically |
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| #2: Protein | Mass: 13708.326 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #3: Water | ChemComp-HOH / |
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.27 Å3/Da / Density % sol: 45.91 % | |||||||||||||||
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| Crystal grow | *PLUS Temperature: 4 ℃ / pH: 5.3 / Method: vapor diffusion, hanging drop | |||||||||||||||
| Components of the solutions | *PLUS
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-Data collection
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
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| Radiation wavelength | Relative weight: 1 |
| Reflection | *PLUS Highest resolution: 2.3 Å / Num. obs: 5664 / Redundancy: 3.9 % / Rmerge(I) obs: 0.129 |
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Processing
| Software | Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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| Refinement | Resolution: 2.32→8 Å / σ(F): 2 Details: OLIGONUCLEOTIDE STEREOCHEMISTRY: NUCLEOTIDE SUGAR PUCKER BASE A1 C2'-ENDO SYN T2 C2'-ENDO ANTI A3 C3'-ENDO ANTI A4 C3'-ENDO ANTI
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| Refinement step | Cycle: LAST / Resolution: 2.32→8 Å
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| Refine LS restraints |
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| Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement | *PLUS Highest resolution: 2.32 Å / Lowest resolution: 8 Å / σ(F): 2 / Rfactor obs: 0.172 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 3.57 |
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