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- PDB-2yg1: APO STRUCTURE OF CELLOBIOHYDROLASE 1 (CEL7A) FROM HETEROBASIDION ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2yg1 | ||||||||||||
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Title | APO STRUCTURE OF CELLOBIOHYDROLASE 1 (CEL7A) FROM HETEROBASIDION ANNOSUM | ||||||||||||
![]() | CELLULOSE 1,4-BETA-CELLOBIOSIDASE | ||||||||||||
![]() | HYDROLASE / GLYCOSIDE HYDROLASE / CELLULASE / WHITE-ROT FUNGUS / BASIDIOMYCETE / FOREST PATHOGEN | ||||||||||||
Function / homology | ![]() Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds / cellulose catabolic process / hydrolase activity, hydrolyzing O-glycosyl compounds / metal ion binding Similarity search - Function | ||||||||||||
Biological species | ![]() | ||||||||||||
Method | ![]() ![]() ![]() | ||||||||||||
![]() | Haddad-Momeni, M. / Hansson, H. / Mikkelsen, N.E. / Wang, X. / Svedberg, J. / Sandgren, M. / Stahlberg, J. | ||||||||||||
![]() | ![]() Title: Structural, Biochemical, and Computational Characterization of the Glycoside Hydrolase Family 7 Cellobiohydrolase of the Tree-Killing Fungus Heterobasidion Irregulare. Authors: Momeni, M.H. / Payne, C.M. / Hansson, H. / Mikkelsen, N.E. / Svedberg, J. / Engstrom, A. / Sandgren, M. / Beckham, G.T. / Stahlberg, J. | ||||||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 195.3 KB | Display | ![]() |
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PDB format | ![]() | 153.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1 MB | Display | ![]() |
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Full document | ![]() | 1 MB | Display | |
Data in XML | ![]() | 42 KB | Display | |
Data in CIF | ![]() | 64.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2xspC ![]() 1z3vS 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: 46991.227 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) ![]() References: UniProt: I1SB08*PLUS, Hydrolases; Glycosylases; Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds #2: Polysaccharide | Source method: isolated from a genetically manipulated source #3: Chemical | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.96 Å3/Da / Density % sol: 37 % / Description: NONE |
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Crystal grow | pH: 7.7 Details: PROTEIN WAS CRYSTALLIZED FROM 20 MM MGCL2, 0.1 M HEPES, PH 7.5, 22% POLYACRYLIC ACID 5100, NA SALT. |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH MAR165 / Detector: CCD / Date: Feb 15, 2010 / Details: MULTILAYER MIRROR |
Radiation | Monochromator: BENT SI CRYSTAL / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.04 Å / Relative weight: 1 |
Reflection | Resolution: 1.9→29.4 Å / Num. obs: 54342 / % possible obs: 98.1 % / Observed criterion σ(I): 3.3 / Redundancy: 4.1 % / Rmerge(I) obs: 0.06 / Net I/σ(I): 15.7 |
Reflection shell | Resolution: 1.9→2 Å / Redundancy: 3.9 % / Rmerge(I) obs: 0.23 / Mean I/σ(I) obs: 5.5 / % possible all: 96.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1Z3V Resolution: 1.9→28.1 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.92 / SU B: 4.495 / SU ML: 0.133 / Cross valid method: THROUGHOUT / ESU R: 0.212 / ESU R Free: 0.182 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY. RESIDUES 45, 46, 47, 52, 53, 54, 55, 197, 198, 199, 200, 201, 202 AND 203 FROM CHAIN B, HAVE NOT BEEN MODELED.
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 20.163 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→28.1 Å
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Refine LS restraints |
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