+Open data
-Basic information
Entry | Database: PDB / ID: 6h1z | ||||||
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Title | AFGH61B WILD-TYPE | ||||||
Components | Endoglucanase, putativeCellulase | ||||||
Keywords | OXIDOREDUCTASE / lytic polysaccharide monooxygenase | ||||||
Function / homology | Function and homology information cellulose binding / cellulase / cellulase activity / cellulose catabolic process / extracellular region Similarity search - Function | ||||||
Biological species | Neosartorya fumigata (mold) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.57 Å | ||||||
Authors | Lo Leggio, L. / Poulsen, J.C.N. | ||||||
Citation | Journal: Carbohydr. Res. / Year: 2018 Title: Structure of a lytic polysaccharide monooxygenase from Aspergillus fumigatus and an engineered thermostable variant. Authors: Lo Leggio, L. / Weihe, C.D. / Poulsen, J.N. / Sweeney, M. / Rasmussen, F. / Lin, J. / De Maria, L. / Wogulis, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6h1z.cif.gz | 111.6 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6h1z.ent.gz | 85.1 KB | Display | PDB format |
PDBx/mmJSON format | 6h1z.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/h1/6h1z ftp://data.pdbj.org/pub/pdb/validation_reports/h1/6h1z | HTTPS FTP |
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-Related structure data
Related structure data | 6ha5C 6haqC 3zudS 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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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 24184.715 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Neosartorya fumigata (mold) / Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100 / Gene: AFUA_4G07850 / Production host: Aspergillus oryzae (mold) References: UniProt: Q4WP32, Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds #2: Chemical | #3: Chemical | ChemComp-ACT / #4: Chemical | ChemComp-NA / | #5: Water | ChemComp-HOH / | |
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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: 1.83 Å3/Da / Density % sol: 32.85 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, sitting drop Details: 0.2 M sodium thiocyanate pH 6.9, 20 %w/v PEG 3350 (reservoir) |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: MAX II / Beamline: I911-3 / Wavelength: 1.1 Å |
Detector | Type: MARMOSAIC 225 mm CCD / Detector: CCD / Date: Aug 24, 2012 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.1 Å / Relative weight: 1 |
Reflection | Resolution: 1.57→20 Å / Num. obs: 43815 / % possible obs: 91.6 % / Redundancy: 2.5 % / Rsym value: 0.041 / Net I/σ(I): 19.5 |
Reflection shell | Resolution: 1.57→1.61 Å / Redundancy: 1.2 % / Mean I/σ(I) obs: 4.9 / Rsym value: 0.136 / % possible all: 51.7 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3ZUD Resolution: 1.57→19.43 Å / Cor.coef. Fo:Fc: 0.975 / Cor.coef. Fo:Fc free: 0.961 / SU B: 1.393 / SU ML: 0.05 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.084 / ESU R Free: 0.085 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: 55.41 Å2 / Biso mean: 14.517 Å2 / Biso min: 7.12 Å2
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Refinement step | Cycle: final / Resolution: 1.57→19.43 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.57→1.611 Å / Total num. of bins used: 20
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