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- PDB-2bvw: CELLOBIOHYDROLASE II (CEL6A) FROM HUMICOLA INSOLENS IN COMPLEX WI... -
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Open data
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Basic information
Entry | Database: PDB / ID: 2bvw | |||||||||
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Title | CELLOBIOHYDROLASE II (CEL6A) FROM HUMICOLA INSOLENS IN COMPLEX WITH GLUCOSE AND CELLOTETRAOSE | |||||||||
![]() | CELLOBIOHYDROLASE II | |||||||||
![]() | HYDROLASE / CELLULOSE DEGRADATION / CELLOBIOHYDROLASE / CELLULASE / GLYCOSIDE HYDROLASE FAMILY 6 | |||||||||
Function / homology | ![]() cellulose 1,4-beta-cellobiosidase (non-reducing end) / cellulose 1,4-beta-cellobiosidase activity / cellulose binding / cellulose catabolic process / extracellular region Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Varrot, A. / Davies, G.J. / Schulein, M. | |||||||||
![]() | ![]() Title: Structural changes of the active site tunnel of Humicola insolens cellobiohydrolase, Cel6A, upon oligosaccharide binding. Authors: Varrot, A. / Schulein, M. / Davies, G.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 | ![]() | 171.7 KB | Display | ![]() |
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PDB format | ![]() | 133.9 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 | ![]() | 18.3 KB | Display | |
Data in CIF | ![]() | 30.2 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1bvwS 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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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (0.51751, -0.05441, 0.85394), Vector: |
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 40014.512 Da / Num. of mol.: 2 / Fragment: CATALYTIC CORE DOMAIN Source method: isolated from a genetically manipulated source Details: N-LINKED N-ACETYLGLUCOSAMINE ON RESIDUE ASN 141 / Source: (gene. exp.) ![]() Plasmid: UNDER CONTROL OF THE FUNGAL AMYLASE PROMOTER AND AMYLOGLUCOSIDASE TERMINATOR Production host: ![]() ![]() References: UniProt: Q9C1S9, cellulose 1,4-beta-cellobiosidase (non-reducing end) |
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-Sugars , 4 types, 6 molecules ![](data/chem/img/NAG.gif)
![](data/chem/img/BGC.gif)
![](data/chem/img/BGC.gif)
#2: Polysaccharide | beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-beta-D-glucopyranose / beta-cellotetraose | ||
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#3: Polysaccharide | beta-D-glucopyranose-(1-4)-beta-D-glucopyranose-(1-4)-alpha-D-glucopyranose / alpha-cellotriose | ||
#4: Sugar | #5: Sugar | |
-Non-polymers , 2 types, 624 molecules ![](data/chem/img/GOL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/HOH.gif)
#6: Chemical | ChemComp-GOL / #7: Water | ChemComp-HOH / | |
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-Details
Nonpolymer details | CELLOTETRAOSE WITH ALPHA AND BETA OXYGENE AT C1 CELLOTRIOSE WITH ALPHA AND BETA OXYGENE AT C1 ...CELLOTETRA |
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Sequence details | THERE IS A PRO-SEQUENCE OF 23 AMINO-ACIDS WHICH ARE POST-TRANSLATIONALLY CLEAVED TO YIELD A MATURE ...THERE IS A PRO-SEQUENCE OF 23 AMINO-ACIDS WHICH ARE POST-TRANSLATIO |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.01 Å3/Da / Density % sol: 38.2 % Description: SEARCH MODEL WAS CEL6A FROM HUMICOLA INSOLENS NATIVE STRUCTURE | ||||||||||||||||||||||||||||||||||||
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Crystal grow | pH: 4.6 / Details: pH 4.6 | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion, hanging dropDetails: drop contains a 50:50(v/v) mix of protein and of reservoir solution | ||||||||||||||||||||||||||||||||||||
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: ADSC QUANTUM 4 / Detector: CCD / Date: Jul 1, 1998 / Details: TORROIDAL MIRROR |
Radiation | Monochromator: SILICON / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.87 Å / Relative weight: 1 |
Reflection | Resolution: 1.7→20 Å / Num. obs: 72987 / % possible obs: 89.6 % / Redundancy: 4.4 % / Rmerge(I) obs: 0.078 / Rsym value: 0.078 / Net I/σ(I): 11.4 |
Reflection shell | Resolution: 1.7→1.79 Å / Redundancy: 4.6 % / Rmerge(I) obs: 0.359 / Mean I/σ(I) obs: 3.9 / Rsym value: 0.359 / % possible all: 89.6 |
Reflection shell | *PLUS % possible obs: 89.6 % / Mean I/σ(I) obs: 1.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1BVW Resolution: 1.7→20 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.7→20 Å
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Refine LS restraints |
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Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor Rfree: 0.225 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |