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Yorodumi- PDB-1eqc: EXO-B-(1,3)-GLUCANASE FROM CANDIDA ALBICANS IN COMPLEX WITH CASTA... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1eqc | ||||||
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Title | EXO-B-(1,3)-GLUCANASE FROM CANDIDA ALBICANS IN COMPLEX WITH CASTANOSPERMINE AT 1.85 A | ||||||
Components | EXO-(B)-(1,3)-GLUCANASE | ||||||
Keywords | HYDROLASE / EXO-GLUCANASE / CANDIDA ALBICANS / MECHANISM-BASED INHIBITORS | ||||||
Function / homology | Function and homology information glucan metabolic process / single-species biofilm formation in or on host organism / glucan 1,3-beta-glucosidase / glucan exo-1,3-beta-glucosidase activity / single-species biofilm formation on inanimate substrate / glucan catabolic process / fungal-type cell wall organization / Transferases; Glycosyltransferases; Hexosyltransferases / cell-substrate adhesion / cell adhesion molecule binding ...glucan metabolic process / single-species biofilm formation in or on host organism / glucan 1,3-beta-glucosidase / glucan exo-1,3-beta-glucosidase activity / single-species biofilm formation on inanimate substrate / glucan catabolic process / fungal-type cell wall organization / Transferases; Glycosyltransferases; Hexosyltransferases / cell-substrate adhesion / cell adhesion molecule binding / extracellular vesicle / transferase activity / cell surface / extracellular region Similarity search - Function | ||||||
Biological species | Candida albicans (yeast) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 1.85 Å | ||||||
Authors | Cutfield, S.M. / Davies, G.J. / Murshudov, G. / Anderson, B.F. / Moody, P.C.E. / Sullivan, P.A. / Cutfield, J.F. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 1999 Title: The structure of the exo-beta-(1,3)-glucanase from Candida albicans in native and bound forms: relationship between a pocket and groove in family 5 glycosyl hydrolases. Authors: Cutfield, S.M. / Davies, G.J. / Murshudov, G. / Anderson, B.F. / Moody, P.C.E. / Sullivan, P.A. / Cutfield, J.F. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1eqc.cif.gz | 92.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1eqc.ent.gz | 75.1 KB | Display | PDB format |
PDBx/mmJSON format | 1eqc.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/eq/1eqc ftp://data.pdbj.org/pub/pdb/validation_reports/eq/1eqc | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 45269.875 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Candida albicans (yeast) / Strain: ATCC 10261 / Production host: Saccharomyces cerevisiae (brewer's yeast) / References: UniProt: P29717, glucan 1,3-beta-glucosidase |
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#2: Chemical | ChemComp-CTS / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.09 Å3/Da / Density % sol: 41.26 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 7.3 Details: HEPES BUFFER, CACL2, PEG8000, pH 7.3, VAPOR DIFFUSION, HANGING DROP, temperature 291K | ||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 35 % | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.4 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 293 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU RU200 / Wavelength: 1.5418 |
Detector | Type: RIGAKU RAXIS II / Detector: IMAGE PLATE / Date: Jun 16, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→33 Å / Num. all: 33191 / Num. obs: 32957 / % possible obs: 99.3 % / Observed criterion σ(F): 1 / Redundancy: 5.3 % / Biso Wilson estimate: 27.7 Å2 / Rmerge(I) obs: 0.039 / Net I/σ(I): 15.3 |
Reflection shell | Resolution: 1.85→1.95 Å / Redundancy: 4.1 % / Rmerge(I) obs: 0.17 / Num. unique all: 4558 / % possible all: 96.9 |
Reflection shell | *PLUS % possible obs: 96.9 % |
-Processing
Software |
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Refinement | Resolution: 1.85→20 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.85→20 Å
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Refine LS restraints |
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