[English] 日本語
![](img/lk-miru.gif)
- PDB-1qao: THE STRUCTURE OF THE RRNA METHYLTRANSFERASE ERMC': IMPLICATIONS F... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1qao | ||||||
---|---|---|---|---|---|---|---|
Title | THE STRUCTURE OF THE RRNA METHYLTRANSFERASE ERMC': IMPLICATIONS FOR THE REACTION MECHANISM | ||||||
![]() | ERMC' METHYLTRANSFERASE | ||||||
![]() | TRANSFERASE / BINARY COMPLEX WITH S-ADENOSYLMETHIONINE | ||||||
Function / homology | ![]() 23S rRNA (adenine2085-N6)-dimethyltransferase / 23S rRNA (adenine(2085)-N(6))-dimethyltransferase activity / rRNA (adenine-N6,N6-)-dimethyltransferase activity / response to antibiotic / RNA binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Schluckebier, G. / Zhong, P. / Stewart, K.D. / Kavanaugh, T.J. / Abad-Zapatero, C. | ||||||
![]() | ![]() Title: The 2.2 A structure of the rRNA methyltransferase ErmC' and its complexes with cofactor and cofactor analogs: implications for the reaction mechanism. Authors: Schluckebier, G. / Zhong, P. / Stewart, K.D. / Kavanaugh, T.J. / Abad-Zapatero, C. #1: ![]() Title: Crystal structure of ErmC', an RNA methyltransferase which mediates antibiotic resistance in bacteria Authors: Bussiere, D.E. / Muchmore, S.W. / Dealwis, C.G. / Schluckebier, G. / Nienaber, V.L. / Edalji, R.P. / Walter, K.A. / Ladror, U.S. / Holzman, T.F. / Abad-Zapatero, C. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 60.9 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 44.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 441.9 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 445.7 KB | Display | |
Data in XML | ![]() | 7 KB | Display | |
Data in CIF | ![]() | 9.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 28955.529 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
---|---|
#2: Chemical | ChemComp-SAM / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.48 Å3/Da / Density % sol: 64.67 % | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.8 Details: PEG 8000, ammonium acetate, pH 7.8 at 298 K, VAPOR DIFFUSION, HANGING DROP | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IIC / Detector: IMAGE PLATE / Date: Jun 11, 1997 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.7→50 Å / Num. all: 11313 / Num. obs: 11313 / % possible obs: 95.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Biso Wilson estimate: 68 Å2 / Rmerge(I) obs: 0.039 / Net I/σ(I): 15.1 |
Reflection shell | Resolution: 2.7→2.8 Å / Redundancy: 3.2 % / Rmerge(I) obs: 0.298 / Num. unique all: 1113 / % possible all: 96.6 |
Reflection | *PLUS Num. measured all: 36172 |
Reflection shell | *PLUS % possible obs: 96.6 % / Mean I/σ(I) obs: 4.4 |
-
Processing
Software |
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.7→50 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
| |||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.7→50 Å
| |||||||||||||||
Refine LS restraints |
| |||||||||||||||
Software | *PLUS Name: CNS / Classification: refinement | |||||||||||||||
Refinement | *PLUS Highest resolution: 2.7 Å / Lowest resolution: 50 Å / σ(F): 0 / Rfactor obs: 0.23 / Rfactor Rwork: 0.23 | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||
Refine LS restraints | *PLUS
|