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- PDB-1qhz: NATIVE TETRAGONAL STRUCTURE OF THE ENDOGLUCANASE CEL5A FROM BACIL... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1qhz | ||||||
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Title | NATIVE TETRAGONAL STRUCTURE OF THE ENDOGLUCANASE CEL5A FROM BACILLUS AGARADHAERENS | ||||||
![]() | ENDOGLUCANASE B | ||||||
![]() | HYDROLASE / CELLULOSE DEGRADATION / ENDOGLUCANASE / GLYCOSHYDROLASE FAMILY 5 | ||||||
Function / homology | ![]() cellulase / cellulase activity / cellulose catabolic process / carbohydrate binding / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Varrot, A. / Schulein, M. / Davies, G.J. | ||||||
![]() | ![]() Title: Insights into ligand-induced conformational change in Cel5A from Bacillus agaradhaerens revealed by a catalytically active crystal form. Authors: Varrot, A. / Schulein, M. / Davies, G.J. | ||||||
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 83.7 KB | Display | ![]() |
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PDB format | ![]() | 60.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 420.5 KB | Display | ![]() |
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Full document | ![]() | 421.7 KB | Display | |
Data in XML | ![]() | 16.2 KB | Display | |
Data in CIF | ![]() | 25 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1qi0C ![]() 1qi2C ![]() 1a3hS 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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2 | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 34156.180 Da / Num. of mol.: 1 / Fragment: CATALYTIC CORE DOMAIN ONLY Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: P06565, UniProt: O85465*PLUS, cellulase | ||||
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#2: Chemical | ChemComp-CA / #3: Water | ChemComp-HOH / | Sequence details | THE SEQUENCE CORRESPONDS TO THE PRECURSOR SEQUENCE OF CEL5A. THE 26 FIRST RESIDUES ARE CLEAVED SO ...THE SEQUENCE CORRESPOND | |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.48 Å3/Da / Density % sol: 50.1 % | ||||||||||||||||||||
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Crystal grow | pH: 7 Details: PROTEIN (20MGML-1) WAS CRYSTALLISED FROM 28% PEG400 AS PRECIPITANT, 100MM TRIETHANOLAMINE AT PH 7.0 AS BUFFER AND 200 MM CACL2 | ||||||||||||||||||||
Crystal grow | *PLUS Temperature: 100 K / Method: vapor diffusion, hanging drop | ||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 120 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Nov 1, 1997 / Details: LONG MIRRORS (MSC) |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→15 Å / Num. obs: 28709 / % possible obs: 100 % / Redundancy: 9 % / Biso Wilson estimate: 20.5 Å2 / Rmerge(I) obs: 0.068 / Rsym value: 6.8 / Net I/σ(I): 31.15 |
Reflection shell | Resolution: 1.95→2.02 Å / Redundancy: 8.8 % / Rmerge(I) obs: 0.311 / Mean I/σ(I) obs: 7.7 / Rsym value: 31.1 / % possible all: 100 |
Reflection shell | *PLUS % possible obs: 100 % |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 1A3H Resolution: 1.95→15 Å / Cross valid method: THROUGHOUT / σ(F): 0
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Displacement parameters | Biso mean: 23 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.95→15 Å
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Refine LS restraints |
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