[English] 日本語
![](img/lk-miru.gif)
- PDB-1anu: COHESIN-2 DOMAIN OF THE CELLULOSOME FROM CLOSTRIDIUM THERMOCELLUM -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1anu | ||||||
---|---|---|---|---|---|---|---|
Title | COHESIN-2 DOMAIN OF THE CELLULOSOME FROM CLOSTRIDIUM THERMOCELLUM | ||||||
![]() | COHESIN-2 | ||||||
![]() | COHESIN / SCAFFOLDING / CELLULOSE DIGESTION / BETA SANDWICH / THERMOPHILE | ||||||
Function / homology | ![]() cellulose binding / cellulose catabolic process / hydrolase activity, hydrolyzing O-glycosyl compounds / cell wall organization / extracellular region Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Shimon, L.J.W. / Yaron, S. / Shoham, Y. / Lamed, R. / Morag, E. / Bayer, E.A. / Frolow, F. | ||||||
![]() | ![]() Title: A cohesin domain from Clostridium thermocellum: the crystal structure provides new insights into cellulosome assembly. Authors: Shimon, L.J. / Bayer, E.A. / Morag, E. / Lamed, R. / Yaron, S. / Shoham, Y. / Frolow, F. #1: ![]() Title: Expression, Purification and Subunit-Binding Properties of Cohesins 2 and 3 of the Clostridium Thermocellum Cellulosome Authors: Yaron, S. / Morag, E. / Bayer, E.A. / Lamed, R. / Shoham, Y. #2: ![]() Title: The Cellulosome--A Treasure-Trove for Biotechnology Authors: Bayer, E.A. / Morag, E. / Lamed, R. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 37.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 25.8 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 14752.648 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: INCORPORATES CELLULOLYTIC ENZYME INTO THE SCAFFOLDING PROTEIN OF CELLULOSOME Source: (gene. exp.) ![]() ![]() ![]() |
---|---|
#2: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.6 Å3/Da / Density % sol: 51 % | ||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | pH: 8.6 / Details: 28% PEG 6000, 750 MM LICL, 100 MM TRIS-HCL, PH 8.6 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Temperature: 19 ℃ / Method: vapor diffusion, hanging drop | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 293 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: RIGAKU / Detector: IMAGE PLATE / Date: May 1, 1996 / Details: MIRRORS |
Radiation | Monochromator: NI FILTER / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.15→30 Å / Num. obs: 8276 / % possible obs: 97.4 % / Observed criterion σ(I): -3 / Redundancy: 5.2 % / Rmerge(I) obs: 0.071 / Rsym value: 0.071 / Net I/σ(I): 31.25 |
Reflection shell | Resolution: 2.15→2.19 Å / Redundancy: 2.5 % / Rmerge(I) obs: 0.283 / Mean I/σ(I) obs: 3.5 / Rsym value: 0.283 / % possible all: 84 |
Reflection | *PLUS Num. measured all: 42676 |
Reflection shell | *PLUS % possible obs: 84 % |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.15→30 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Highest resolution: 2.15 Å / Rfactor Rfree: 0.369 / Rfactor Rwork: 0.351 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | *PLUS Rfactor obs: 0.351 |