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Yorodumi- PDB-1ghs: THE THREE-DIMENSIONAL STRUCTURES OF TWO PLANT BETA-GLUCAN ENDOHYD... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1ghs | ||||||
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Title | THE THREE-DIMENSIONAL STRUCTURES OF TWO PLANT BETA-GLUCAN ENDOHYDROLASES WITH DISTINCT SUBSTRATE SPECIFICITIES | ||||||
Components | 1,3-BETA-GLUCANASE | ||||||
Keywords | HYDROLASE | ||||||
Function / homology | Function and homology information (1->3)-beta-D-glucan catabolic process / glucan endo-1,3-beta-D-glucosidase / glucan endo-1,3-beta-D-glucosidase activity / defense response to fungus Similarity search - Function | ||||||
Biological species | Hordeum vulgare (barley) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Garrett, T.P.J. / Varghese, J.N. | ||||||
Citation | Journal: Proc.Natl.Acad.Sci.USA / Year: 1994 Title: Three-dimensional structures of two plant beta-glucan endohydrolases with distinct substrate specificities. Authors: Varghese, J.N. / Garrett, T.P. / Colman, P.M. / Chen, L. / Hoj, P.B. / Fincher, G.B. #1: Journal: J.Mol.Biol. / Year: 1993 Title: Crystallization and Preliminary X-Ray Analysis of (1,3)-and (1,3;1,4)-Beta--D-Glucanases from Germinating Barley Authors: Chen, L. / Garrett, T.P.J. / Varghese, J.N. / Fincher, G.B. / Hoj, P.B. #2: Journal: J.Biol.Chem. / Year: 1993 Title: Evolution of Polysaccharide Hydrolase Substrate Specificity Authors: Chen, L. / Fincher, G.B. / Hoj, P.J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1ghs.cif.gz | 121.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1ghs.ent.gz | 96.2 KB | Display | PDB format |
PDBx/mmJSON format | 1ghs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gh/1ghs ftp://data.pdbj.org/pub/pdb/validation_reports/gh/1ghs | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Atom site foot note | 1: CIS PROLINE - PRO A 82 / 2: CIS PROLINE - PRO A 138 3: PHE A 274 - ALA A 275 OMEGA = 0.24 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION 4: CIS PROLINE - PRO B 82 / 5: CIS PROLINE - PRO B 138 6: PHE B 274 - ALA B 275 OMEGA = 0.07 PEPTIDE BOND DEVIATES SIGNIFICANTLY FROM TRANS CONFORMATION | ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.4929, 0.8692, -0.0394), Vector: |
-Components
#1: Protein | Mass: 32377.180 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Hordeum vulgare (barley) References: UniProt: P15737, glucan endo-1,3-beta-D-glucosidase #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.62 Å3/Da / Density % sol: 53.14 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 4 ℃ / pH: 7.5 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
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: 1.8 Å / Num. obs: 32509 / % possible obs: 78.4 % / Num. measured all: 114164 / Rmerge(I) obs: 0.098 |
-Processing
Software |
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Refinement | Resolution: 2.3→6 Å / σ(F): 4 /
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Refinement step | Cycle: LAST / Resolution: 2.3→6 Å
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Refine LS restraints |
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Software | *PLUS Name: X-PLOR / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.179 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_angle_d / Dev ideal: 1.68 |