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Open data
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Basic information
| Entry | Database: PDB / ID: 1cnv | ||||||
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| Title | CRYSTAL STRUCTURE OF CONCANAVALIN B AT 1.65 A RESOLUTION | ||||||
Components | CONCANAVALIN B | ||||||
Keywords | SEED PROTEIN / PLANT CHITINASE / CHITIN BINDING PROTEIN | ||||||
| Function / homology | Function and homology informationchitinase activity / carbohydrate metabolic process / extracellular region Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | X-RAY DIFFRACTION / Resolution: 1.65 Å | ||||||
Authors | Hennig, M. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1995Title: Crystal structure of concanavalin B at 1.65 A resolution. An "inactivated" chitinase from seeds of Canavalia ensiformis. Authors: Hennig, M. / Jansonius, J.N. / Terwisscha van Scheltinga, A.C. / Dijkstra, B.W. / Schlesier, B. #1: Journal: To be PublishedTitle: Sequence Analysis of Concanavalin B from Canavalia Ensiformis Reveals Homology to Chitinases Authors: Schlesier, B. / Nong, V.H. / Horstmann, C.H. / Hennig, M. | ||||||
| History |
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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 | 1cnv.cif.gz | 74.9 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1cnv.ent.gz | 55.4 KB | Display | PDB format |
| PDBx/mmJSON format | 1cnv.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cn/1cnv ftp://data.pdbj.org/pub/pdb/validation_reports/cn/1cnv | HTTPS FTP |
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-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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| Atom site foot note | 1: SER 34 - PHE 35 OMEGA = 11.26 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 2: PRO 56 - SER 57 OMEGA = 127.50 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 3: CIS PROLINE - PRO 168 / 4: CIS PROLINE - PRO 217 5: TRP 265 - ASN 266 OMEGA = 0.41 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION |
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Components
| #1: Protein | Mass: 33866.258 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #2: Water | ChemComp-HOH / |
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION |
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Sample preparation
| Crystal | Density Matthews: 2.88 Å3/Da / Density % sol: 57.36 % |
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| Crystal grow | *PLUS Method: microdialysis |
-Data collection
| Diffraction source | Wavelength: 1.54 |
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| Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Dec 13, 1993 |
| Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
| Reflection | Resolution: 1.65→15 Å / Num. obs: 40387 / % possible obs: 85.9 % / Observed criterion σ(I): 0 / Redundancy: 3.9 % / Rmerge(I) obs: 0.042 |
| Reflection | *PLUS Num. measured all: 145907 / Rmerge(I) obs: 0.0042 |
| Reflection shell | *PLUS Highest resolution: 1.65 Å / Lowest resolution: 1.74 Å / % possible obs: 64.1 % / Redundancy: 2.9 % / Rmerge(I) obs: 0.23 / Mean I/σ(I) obs: 3.4 |
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Processing
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| Refinement | Resolution: 1.65→10 Å / σ(F): 0
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| Displacement parameters | Biso mean: 17.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 1.65→10 Å
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| Refine LS restraints |
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| Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Displacement parameters | *PLUS |
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