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- PDB-1oa4: Comparison of Family 12 Glycoside Hydrolases and Recruited Substi... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1oa4 | ||||||
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Title | Comparison of Family 12 Glycoside Hydrolases and Recruited Substitutions Important for Thermal Stability | ||||||
![]() | ENDO-BETA-1,4-GLUCANASE | ||||||
![]() | HYDROLASE / CELLULASE / CELLULOSE DEGRADATION / ENDOGLUCANASE / GLYCOSYL HYDROLASE / GH FAMILY 12 / STREPTOMYCES SP 11AG8 CEL12A | ||||||
Function / homology | ![]() polysaccharide binding / cellulase activity / polysaccharide catabolic process Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Sandgren, M. / Gualfetti, P.J. / Shaw, A. / Gross, L.S. / Saldajeno, M. / Day, A.G. / Jones, T.A. / Mitchinson, C. | ||||||
![]() | ![]() Title: Comparison of Family 12 Glycoside Hydrolases and Recruited Substitutions Important for Thermal Stability Authors: Sandgren, M. / Gualfetti, P.J. / Shaw, A. / Gross, L.S. / Saldajeno, M. / Day, A.G. / Jones, T.A. / Mitchinson, C. | ||||||
History |
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Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 56.1 KB | Display | ![]() |
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PDB format | ![]() | 39.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 421.1 KB | Display | ![]() |
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Full document | ![]() | 423.6 KB | Display | |
Data in XML | ![]() | 11.2 KB | Display | |
Data in CIF | ![]() | 15.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1oa2C ![]() 1oa3C ![]() 1nlrS C: citing same article ( S: Starting model for refinement |
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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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Unit cell |
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Components
#1: Protein | Mass: 23890.135 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN, RESIDUES 32-253 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.2 Å3/Da / Density % sol: 44 % | ||||||||||||||||||||||||
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Crystal grow | pH: 6 / Details: pH 6.00 | ||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 25 ℃ / Method: vapor diffusion, sitting drop / PH range low: 6 / PH range high: 5 | ||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MSC / Detector: IMAGE PLATE / Date: Feb 15, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 1.5→29 Å / Num. obs: 26559 / % possible obs: 73 % / Observed criterion σ(I): 3 / Redundancy: 2.3 % / Rsym value: 0.054 / Net I/σ(I): 15.4 |
Reflection shell | Resolution: 1.5→1.53 Å / Mean I/σ(I) obs: 8.6 / Rsym value: 0.161 / % possible all: 63.5 |
Reflection | *PLUS Lowest resolution: 29 Å / % possible obs: 72.9 % / Redundancy: 3.3 % / Num. measured all: 88448 / Rmerge(I) obs: 0.054 |
Reflection shell | *PLUS % possible obs: 63.5 % / Rmerge(I) obs: 0.161 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1NLR Resolution: 1.5→29 Å / SU B: 2.08226 / SU ML: 0.07506 / Cross valid method: THROUGHOUT / σ(F): 0 / ESU R: 0.16547 / ESU R Free: 0.1227 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Displacement parameters | Biso mean: 14.276 Å2
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Refinement step | Cycle: LAST / Resolution: 1.5→29 Å
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Refinement | *PLUS Rfactor Rfree: 0.193 / Rfactor Rwork: 0.181 | ||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||
Refine LS restraints | *PLUS
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