[English] 日本語
![](img/lk-miru.gif)
- PDB-2cc0: Family 4 carbohydrate esterase from Streptomyces lividans in comp... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2cc0 | ||||||
---|---|---|---|---|---|---|---|
Title | Family 4 carbohydrate esterase from Streptomyces lividans in complex with acetate | ||||||
![]() | ACETYL-XYLAN ESTERASE | ||||||
![]() | ![]() | ||||||
Function / homology | ![]() hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds / ![]() ![]() Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Taylor, E.J. / Gloster, T.M. / Turkenburg, J.P. / Vincent, F. / Brzozowski, A.M. / Dupont, C. / Shareck, F. / Centeno, M.S.J. / Prates, J.A.M. / Puchart, V. ...Taylor, E.J. / Gloster, T.M. / Turkenburg, J.P. / Vincent, F. / Brzozowski, A.M. / Dupont, C. / Shareck, F. / Centeno, M.S.J. / Prates, J.A.M. / Puchart, V. / Ferreira, L.M.A. / Fontes, C.M.G.A. / Biely, P. / Davies, G.J. | ||||||
![]() | ![]() Title: Structure and Activity of Two Metal-Ion Dependent Acetyl Xylan Esterases Involved in Plant Cell Wall Degradation Reveals a Close Similarity to Peptidoglycan Deacetylases Authors: Taylor, E.J. / Gloster, T.M. / Turkenburg, J.P. / Vincent, F. / Brzozowski, A.M. / Dupont, C. / Shareck, F. / Centeno, M.S.J. / Prates, J.A.M. / Puchart, V. / Ferreira, L.M.A. / Fontes, C.M. ...Authors: Taylor, E.J. / Gloster, T.M. / Turkenburg, J.P. / Vincent, F. / Brzozowski, A.M. / Dupont, C. / Shareck, F. / Centeno, M.S.J. / Prates, J.A.M. / Puchart, V. / Ferreira, L.M.A. / Fontes, C.M.G.A. / Biely, P. / Davies, G.J. | ||||||
History |
| ||||||
Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN ... SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SHEETS ARE DEFINED. |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 183.1 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 145.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
---|
-Related structure data
Related structure data | ![]() 2c71SC ![]() 2c79C S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
| ||||||||
Noncrystallographic symmetry (NCS) | NCS oper: (Code: given Matrix: (-0.99967, -0.00044, -0.02584), Vector ![]() |
-
Components
#1: Protein | Mass: 20614.910 Da / Num. of mol.: 2 / Fragment: RESIDUES 42-236 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() ![]() #2: Chemical | #3: Chemical | ![]() #4: Water | ChemComp-HOH / | ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.05 Å3/Da / Density % sol: 39.39 % |
---|---|
Crystal grow![]() | pH: 4.5 Details: 7-13% PEG 4K, 0.2 M KBR, 0.1 M NAAC, PH 4.5. PROTEIN 20 MG/ML. |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Details: TOROIDAL MIRROR |
Radiation | Monochromator: SI (311) MONOCHROMATOR AND SI(111) MONOCHROMATOR Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength![]() |
Reflection | Resolution: 1.6→40 Å / Num. obs: 51014 / % possible obs: 98 % / Redundancy: 3.4 % / Rmerge(I) obs: 0.05 / Net I/σ(I): 17 |
Reflection shell | Resolution: 1.6→1.66 Å / Redundancy: 2.8 % / Rmerge(I) obs: 0.26 / Mean I/σ(I) obs: 4 / % possible all: 91 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure![]() ![]() Starting model: PDB ENTRY 2C71 Resolution: 1.6→65.65 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.955 / SU B: 2.893 / SU ML: 0.047 / Cross valid method: THROUGHOUT / ESU R: 0.108 / ESU R Free: 0.082 / Stereochemistry target values: MAXIMUM LIKELIHOOD
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 16.32 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 1.6→65.65 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|