+Open data
-Basic information
Entry | Database: PDB / ID: 1gon | ||||||
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Title | b-glucosidase from Streptomyces sp | ||||||
Components | BETA-GLUCOSIDASE | ||||||
Keywords | HYDROLASE / GLYCOSYLTRANSFERASE / FAMILY 1 OF GLYCOSYL HYDROLASE | ||||||
Function / homology | Function and homology information : / beta-glucosidase / beta-glucosidase activity / cellulose catabolic process Similarity search - Function | ||||||
Biological species | STREPTOMYCES SP. (bacteria) | ||||||
Method | X-RAY DIFFRACTION / MOLECULAR REPLACEMENT / Resolution: 2.2 Å | ||||||
Authors | Guasch, A. / Perez-Pons, J.A. / Vallmitjana, M. / Querol, E. / Coll, M. | ||||||
Citation | Journal: To be Published Title: Crystal Structure of a Family 1 Beta-Glucosidase from Streptomyces Authors: Guasch, A. / Vallmitjana, M. / Perez, R. / Querol, E. / Perez-Pons, J.A. / Coll, M. #1: Journal: Acta Crystallogr.,Sect.D / Year: 1999 Title: Cloning, Overexpression, Crystallization and Preliminary X-Ray Analysis of a Family 1 Beta--Glucosidase from Streptomyces Authors: Guash, A. / Vallmitjana, M. / Perez, R. / Querol, E. / Peez-Pons, J.A. / Coll, M. | ||||||
History |
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Remark 700 | SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW ... SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "AB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 8-STRANDED BARREL THIS IS REPRESENTED BY A 9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. |
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1gon.cif.gz | 190.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1gon.ent.gz | 151 KB | Display | PDB format |
PDBx/mmJSON format | 1gon.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1gon_validation.pdf.gz | 384.7 KB | Display | wwPDB validaton report |
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Full document | 1gon_full_validation.pdf.gz | 394.2 KB | Display | |
Data in XML | 1gon_validation.xml.gz | 18.4 KB | Display | |
Data in CIF | 1gon_validation.cif.gz | 30.9 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/go/1gon ftp://data.pdbj.org/pub/pdb/validation_reports/go/1gon | HTTPS FTP |
-Related structure data
Related structure data | 1gnxS S: Starting model for refinement |
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Similar 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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-Components
#1: Protein | Mass: 52378.992 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) STREPTOMYCES SP. (bacteria) / Production host: ESCHERICHIA COLI (E. coli) / References: UniProt: Q59976 #2: Chemical | ChemComp-HG / #3: Chemical | #4: Water | ChemComp-HOH / | Compound details | THE PROTEIN WAS SUBMITED TO LIMITED PROTEOLYSIS WITH TRYPSIN. THE MAJOR TRYPSIN-CLEAVAGE SITES ...THE PROTEIN WAS SUBMITED TO LIMITED PROTEOLYSI | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.48 Å3/Da / Density % sol: 48.03 % |
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Crystal grow | pH: 7.5 / Details: 1.9 M AMMONIUM SULFATE, 0.1 M HEPES PH 7. |
-Data collection
Diffraction | Mean temperature: 103 K |
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Diffraction source | Source: ROTATING ANODE / Type: RIGAKU / Wavelength: 1.53 |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.53 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→40 Å / Num. obs: 48407 / % possible obs: 95.4 % / Observed criterion σ(I): 0 / Redundancy: 98.1 % / Rmerge(I) obs: 0.081 / Net I/σ(I): 29.1 |
Reflection shell | Resolution: 2.2→2.24 Å / Redundancy: 81.5 % / Rmerge(I) obs: 0.221 / Mean I/σ(I) obs: 9.32 / % possible all: 98.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1GNX Resolution: 2.2→40 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 77.5029 Å2
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Refinement step | Cycle: LAST / Resolution: 2.2→40 Å
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Refine LS restraints |
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