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- PDB-2baa: THE REFINED CRYSTAL STRUCTURE OF AN ENDOCHITINASE FROM HORDEUM VU... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2baa | |||||||||
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Title | THE REFINED CRYSTAL STRUCTURE OF AN ENDOCHITINASE FROM HORDEUM VULGARE L. SEEDS TO 1.8 ANGSTROMS RESOLUTION | |||||||||
![]() | ENDOCHITINASE (26 KD) | |||||||||
![]() | HYDROLASE (O-GLYCOSYL) | |||||||||
Function / homology | ![]() chitinase / chitinase activity / chitin catabolic process / polysaccharide catabolic process / defense response to fungus / cell wall macromolecule catabolic process Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() | |||||||||
![]() | Hart, P.J. / Pfluger, H.D. / Monzingo, A.F. / Ready, M.P. / Ernst, S.R. / Hollis, T. / Robertus, J.D. | |||||||||
![]() | ![]() Title: The refined crystal structure of an endochitinase from Hordeum vulgare L. seeds at 1.8 A resolution. Authors: Hart, P.J. / Pfluger, H.D. / Monzingo, A.F. / Hollis, T. / Robertus, J.D. #1: ![]() Title: Crystal Structure of an Endochitinase from Hordeum Vulgare L. Seeds Authors: Hart, P.J. / Monzingo, A.F. / Ready, M.P. / Ernst, S.R. / Robertus, J.D. #2: ![]() Title: Crystallization of an Endochitinase from Hordeum Vulgare L. Seeds Authors: Hart, P.J. / Ready, M.P. / Robertus, J.D. #3: ![]() Title: Biochemical and Molecular Characterization of Three Barley Seed Proteins with Antifungal Properties Authors: Leah, R. / Tommerup, H. / Svendsen, I. / Mundy, J. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 58.7 KB | Display | ![]() |
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PDB format | ![]() | 43.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 418.8 KB | Display | ![]() |
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Full document | ![]() | 425.7 KB | Display | |
Data in XML | ![]() | 12.8 KB | Display | |
Data in CIF | ![]() | 17.7 KB | Display | |
Arichive directory | ![]() ![]() | 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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Atom site foot note | 1: CIS PROLINE - PRO 164 |
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Components
#1: Protein | Mass: 25955.875 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: 26 KD / Source: (natural) ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.77 % | ||||||||||||||||||||
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Crystal grow | *PLUS pH: 8.5 / Method: vapor diffusion, hanging drop / Details: microseeding | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Reflection | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 3.88 Å / Num. obs: 18975 / % possible obs: 94 % / Num. measured all: 168007 / Rmerge(I) obs: 0.0769 |
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Reflection shell | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 1.86 Å / % possible obs: 98 % / Num. unique obs: 1936 / Num. measured obs: 13313 / Rmerge(I) obs: 0.2091 |
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Processing
Software |
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Refinement | Resolution: 1.8→5 Å / Rfactor Rwork: 0.18 | ||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.8→5 Å
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Refine LS restraints |
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Refinement | *PLUS Rfactor obs: 0.18 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS |