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Open data
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Basic information
Entry | Database: PDB / ID: 6fhw | |||||||||
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Title | Structure of Hormoconis resinae Glucoamylase | |||||||||
![]() | Glucoamylase P | |||||||||
![]() | HYDROLASE / glycosylation / starch degradation / glycoside hydrolase | |||||||||
Function / homology | ![]() glucan 1,4-alpha-glucosidase / glucan 1,4-alpha-glucosidase activity / starch binding / polysaccharide catabolic process / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Roth, C. / Moroz, O.V. / Ariza, A. / Friis, E.P. / Davies, G.J. / Wilson, K.S. | |||||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 239.2 KB | Display | ![]() |
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PDB format | ![]() | 193.6 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 3.8 MB | Display | ![]() |
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Full document | ![]() | 3.8 MB | Display | |
Data in XML | ![]() | 41.1 KB | Display | |
Data in CIF | ![]() | 56.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 6fhvC ![]() 6frvC ![]() 1glmS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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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.) ![]() ![]() #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: ![]() |
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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: ![]() ![]() ![]() |
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 |
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Processing
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Refinement | Method to determine structure: ![]() 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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