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Open data
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Basic information
Entry | Database: PDB / ID: 1cb2 | ||||||
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Title | CELLOBIOHYDROLASE II, CATALYTIC DOMAIN, MUTANT Y169F | ||||||
![]() | CELLOBIOHYDROLASE II | ||||||
![]() | HYDROLASE (O-GLYCOSYL) / GLYCOSIDASE / GLYCOPROTEIN | ||||||
Function / homology | ![]() cellulose 1,4-beta-cellobiosidase (non-reducing end) / cellulose 1,4-beta-cellobiosidase activity / cellulose binding / cellulose catabolic process / extracellular region / identical protein binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() | ||||||
![]() | Kleywegt, G.J. / Szardenings, M. / Jones, T.A. | ||||||
![]() | ![]() Title: The active site of Trichoderma reesei cellobiohydrolase II: the role of tyrosine 169. Authors: Koivula, A. / Reinikainen, T. / Ruohonen, L. / Valkeajarvi, A. / Claeyssens, M. / Teleman, O. / Kleywegt, G.J. / Szardenings, M. / Rouvinen, J. / Jones, T.A. / Teeri, T.T. #1: ![]() Title: Three-Dimensional Structure of Cellobiohydrolase II from Trichoderma Reesei Authors: Rouvinen, J. / Bergfors, T. / Teeri, T. / Knowles, J.K. / Jones, T.A. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 141.7 KB | Display | ![]() |
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PDB format | ![]() | 119.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 465.3 KB | Display | ![]() |
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Full document | ![]() | 467.8 KB | Display | |
Data in XML | ![]() | 31 KB | Display | |
Data in CIF | ![]() | 44.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.994635, -0.096273, -0.037846), Vector: |
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Components
#1: Protein | Mass: 39039.297 Da / Num. of mol.: 2 / Fragment: CATALYTIC / Mutation: Y169F Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P07987, cellulose 1,4-beta-cellobiosidase (non-reducing end) #2: Sugar | ChemComp-NAG / #3: Sugar | ChemComp-MAN / #4: Water | ChemComp-HOH / | Compound details | THE CATALYTIC CORE STARTS AT RESIDUE 83. | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.15 Å3/Da / Density % sol: 42.91 % | ||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 6 / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Wavelength: 1.5418 |
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Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: Apr 2, 1993 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Num. obs: 46849 / % possible obs: 91.7 % / Redundancy: 4.3 % / Rmerge(I) obs: 0.068 |
Reflection | *PLUS Highest resolution: 1.8 Å / Num. measured all: 202105 |
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Processing
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Refinement | Resolution: 2→8 Å / σ(F): 0
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Displacement parameters | Biso mean: 15.8 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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