+Open data
-Basic information
Entry | Database: PDB / ID: 6fhw | |||||||||
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Title | Structure of Hormoconis resinae Glucoamylase | |||||||||
Components | Glucoamylase P | |||||||||
Keywords | HYDROLASE / glycosylation / starch degradation / glycoside hydrolase | |||||||||
Function / homology | Function and homology information glucan 1,4-alpha-glucosidase / glucan 1,4-alpha-glucosidase activity / starch binding / polysaccharide catabolic process / extracellular region Similarity search - Function | |||||||||
Biological species | Amorphotheca resinae (creosote fungus) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.6 Å | |||||||||
Authors | Roth, C. / Moroz, O.V. / Ariza, A. / Friis, E.P. / Davies, G.J. / Wilson, K.S. | |||||||||
Citation | Journal: Acta Crystallogr D Struct Biol / Year: 2018 Title: Structural insight into industrially relevant glucoamylases: flexible positions of starch-binding domains. Authors: Roth, C. / Moroz, O.V. / Ariza, A. / Skov, L.K. / Ayabe, K. / Davies, G.J. / Wilson, K.S. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6fhw.cif.gz | 239.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6fhw.ent.gz | 193.6 KB | Display | PDB format |
PDBx/mmJSON format | 6fhw.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fh/6fhw ftp://data.pdbj.org/pub/pdb/validation_reports/fh/6fhw | HTTPS FTP |
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-Related structure data
Related structure data | 6fhvC 6frvC 1glmS S: Starting model for refinement C: citing same article (ref.) |
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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: 66470.852 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Amorphotheca resinae (creosote fungus) / Gene: GAMP / Production host: Trichoderma reesei QM6a (fungus) / References: UniProt: Q03045, glucan 1,4-alpha-glucosidase #2: Polysaccharide | 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose Source method: isolated from a genetically manipulated source #3: Polysaccharide | alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2- ...alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose | Source method: isolated from a genetically manipulated source #4: Polysaccharide | #5: Sugar | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / Details: tacsimate |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-2 / Wavelength: 0.933 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: May 19, 2010 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.933 Å / Relative weight: 1 |
Reflection | Resolution: 3.6→59.58 Å / Num. obs: 38033 / % possible obs: 81.6 % / Redundancy: 6.5 % / Rrim(I) all: 0.142 / Net I/σ(I): 10.5 |
Reflection shell | Resolution: 3.6→3.76 Å / Rrim(I) all: 0.675 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 1GLM Resolution: 3.6→59.58 Å / Cor.coef. Fo:Fc: 0.82 / Cor.coef. Fo:Fc free: 0.797 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R Free: 0.559 Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 108.24 Å2 / Biso mean: 54.06 Å2 / Biso min: 31.04 Å2
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Refinement step | Cycle: final / Resolution: 3.6→59.58 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 3.6→3.693 Å / Total num. of bins used: 20
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