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Open data
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Basic information
Entry | Database: PDB / ID: 1nlr | ||||||
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Title | ENDO-1,4-BETA-GLUCANASE CELB2, CELLULASE, NATIVE STRUCTURE | ||||||
![]() | ENDO-1,4-BETA-GLUCANASE | ||||||
![]() | ENDOGLUCANASE / GLYCOSYL HYDROLASE / FAMILY 12 / CELB2 | ||||||
Function / homology | ![]() cellulase activity / polysaccharide binding / polysaccharide catabolic process Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Sulzenbacher, G. / Dupont, C. / Davies, G.J. | ||||||
![]() | ![]() Title: The Streptomyces lividans family 12 endoglucanase: construction of the catalytic cre, expression, and X-ray structure at 1.75 A resolution. Authors: Sulzenbacher, G. / Shareck, F. / Morosoli, R. / Dupont, C. / Davies, G.J. #1: ![]() Title: Erratum. Structure of the Inhibitory Receptor for Human Natural Killer Cells Resembles Haematopoietic Receptors Authors: Fan, Q.R. / Mosyak, L. / Winter, C.C. / Wagtmann, N. / Long, E.O. / Wiley, D.C. #2: ![]() Title: Purification and Characterization of the Celb Endoglucanase from Streptomyces Lividans 66 and DNA Sequence of the Encoding Gene Authors: Wittmann, S. / Shareck, F. / Kluepfel, D. / Morosoli, R. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 56.5 KB | Display | ![]() |
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PDB format | ![]() | 43.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-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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Unit cell |
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Components
#1: Protein | Mass: 24594.713 Da / Num. of mol.: 1 / Fragment: CATALYTIC DOMAIN Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Water | ChemComp-HOH / |
Compound details | THE COORDINATES GIVEN DEFINE THE STRUCTURE OF CELB2, THE TRUNCATED, CATALYTICALLY COMPETENT, FORM ...THE COORDINATE |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.01 Å3/Da / Density % sol: 38.2 % | ||||||||||||||||||||
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Crystal grow | Method: vapor diffusion / pH: 4.5 Details: 30 % PEG 1500, PH 4.5 FOR ACETATE BUFFER METHOD: HANGING DROP VAPOUR DIFFUSION, vapor diffusion | ||||||||||||||||||||
Crystal grow | *PLUS 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: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Feb 17, 1997 / Details: FOCUSING MIRRORS |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 1.75→15 Å / Num. obs: 18747 / % possible obs: 95.6 % / Redundancy: 6.98 % / Biso Wilson estimate: 18.51 Å2 / Rmerge(I) obs: 0.047 / Net I/σ(I): 31.4 |
Reflection shell | Resolution: 1.75→1.78 Å / Redundancy: 3.21 % / Rmerge(I) obs: 0.245 / Mean I/σ(I) obs: 5.96 / % possible all: 68.5 |
Reflection | *PLUS % possible obs: 93.7 % / Redundancy: 6.77 % |
Reflection shell | *PLUS Lowest resolution: 1.84 Å / % possible obs: 67.9 % / Redundancy: 2.78 % / Rmerge(I) obs: 0.287 |
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Processing
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Refinement | Method to determine structure: ![]()
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Displacement parameters | Biso mean: 20.4 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.75→15 Å
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Refine LS restraints |
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Software | *PLUS Name: REFMAC / Classification: refinement | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS Rfactor obs: 0.187 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS |