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Yorodumi- PDB-1hvq: CRYSTAL STRUCTURES OF HEVAMINE, A PLANT DEFENCE PROTEIN WITH CHIT... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1hvq | |||||||||
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Title | CRYSTAL STRUCTURES OF HEVAMINE, A PLANT DEFENCE PROTEIN WITH CHITINASE AND LYSOZYME ACTIVITY, AND ITS COMPLEX WITH AN INHIBITOR | |||||||||
Components | HEVAMINE A | |||||||||
Keywords | HYDROLASE / GLYCOSIDASE / CHITIN DEGRADATION / MULTIFUNCTIONAL ENZYME | |||||||||
Function / homology | Function and homology information chitinase / chitinase activity / vacuole / chitin catabolic process / polysaccharide catabolic process / lysozyme / lysozyme activity Similarity search - Function | |||||||||
Biological species | Hevea brasiliensis (rubber tree) | |||||||||
Method | X-RAY DIFFRACTION / Resolution: 2.2 Å | |||||||||
Authors | Terwisscha Van Scheltinga, A.C. / Kalk, K.H. / Beintema, J.J. / Dijkstra, B.W. | |||||||||
Citation | Journal: Structure / Year: 1994 Title: Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor. Authors: Terwisscha van Scheltinga, A.C. / Kalk, K.H. / Beintema, J.J. / Dijkstra, B.W. #1: Journal: J.Mol.Biol. / Year: 1990 Title: Crystallization of Hevamine, an Enzyme with Lysozyme(Slash)Chitinase Activity from Hevea Brasiliensis Latex Authors: Rozeboom, H.J. / Budiani, A. / Beintema, J.J. / Dijkstra, B.W. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1hvq.cif.gz | 66.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1hvq.ent.gz | 51 KB | Display | PDB format |
PDBx/mmJSON format | 1hvq.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hv/1hvq ftp://data.pdbj.org/pub/pdb/validation_reports/hv/1hvq | 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: CIS PROLINE - PRO 162 |
-Components
#1: Protein | Mass: 29573.182 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: PLANT ENDOCHITINASE/LYSOZYME / Source: (natural) Hevea brasiliensis (rubber tree) / Tissue: LATEX / References: UniProt: P23472, chitinase, lysozyme |
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#2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2- ...2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose / triacetyl-beta-chitotriose |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 41.31 % | ||||||||||||||||||
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Crystal grow | *PLUS Method: vapor diffusion, hanging drop / PH range low: 9 / PH range high: 5 | ||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.54 |
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Detector | Type: ENRAF-NONIUS FAST / Detector: DIFFRACTOMETER / Date: Nov 15, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Num. obs: 9453 / % possible obs: 92 % / Observed criterion σ(I): 3 / Redundancy: 3.9 % / Rmerge(I) obs: 0.082 |
Reflection | *PLUS Highest resolution: 2.4 Å / Lowest resolution: 28 Å / Rmerge(I) obs: 0.082 |
-Processing
Software |
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Refinement | Resolution: 2.2→8 Å / σ(F): 0
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Refine analyze | Luzzati coordinate error obs: 0.25 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Highest resolution: 2.4 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |