[English] 日本語
![](img/lk-miru.gif)
- PDB-2wpw: Tandem GNAT protein from the clavulanic acid biosynthesis pathway... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2wpw | ||||||
---|---|---|---|---|---|---|---|
Title | Tandem GNAT protein from the clavulanic acid biosynthesis pathway (without AcCoA) | ||||||
![]() | ORF14 | ||||||
![]() | TRANSFERASE / ACETYL TRANSFERASE / ANTIBIOTIC BIOSYNTHESIS | ||||||
Function / homology | ![]() clavulanic acid biosynthetic process / acyltransferase activity, transferring groups other than amino-acyl groups Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Iqbal, A. / Arunlanantham, H. / McDonough, M.A. / Chowdhury, R. / Clifton, I.J. | ||||||
![]() | ![]() Title: Crystallographic and mass spectrometric analyses of a tandem GNAT protein from the clavulanic acid biosynthesis pathway. Authors: Iqbal, A. / Arunlanantham, H. / Brown, T. / Chowdhury, R. / Clifton, I.J. / Kershaw, N.J. / Hewitson, K.S. / McDonough, M.A. / Schofield, C.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 | ![]() | 282.7 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 242 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.7 MB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 1.8 MB | Display | |
Data in XML | ![]() | 69.2 KB | Display | |
Data in CIF | ![]() | 96.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||||||||||
2 | ![]()
| ||||||||||||||||
3 | ![]()
| ||||||||||||||||
4 | ![]()
| ||||||||||||||||
Unit cell |
| ||||||||||||||||
Noncrystallographic symmetry (NCS) | NCS oper:
|
-
Components
#1: Protein | Mass: 36664.973 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Details: SELENO-METHIONINE LABELLED / Source: (gene. exp.) ![]() ![]() ![]() References: UniProt: Q8KRB5, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups #2: Chemical | ChemComp-ACO / #3: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.05 Å3/Da / Density % sol: 59.7 % / Description: NONE |
---|---|
Crystal grow | pH: 6 Details: 3 MG/ML PROTEIN, 10% PEG8000, 0.1M CACODYLATE PH6, 0.2M SODIUM ACETATE |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Sep 9, 2003 / Details: RH COATED MIRRORS |
Radiation | Monochromator: SI (1 1 1) / Protocol: MAD / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97976 Å / Relative weight: 1 |
Reflection | Resolution: 2.38→32.4 Å / Num. obs: 68408 / % possible obs: 92.2 % / Observed criterion σ(I): 0 / Redundancy: 4.6 % / Biso Wilson estimate: 44.8 Å2 / Rmerge(I) obs: 0.13 / Net I/σ(I): 6.5 |
Reflection shell | Resolution: 2.38→2.51 Å / Redundancy: 4.2 % / Rmerge(I) obs: 0.35 / Mean I/σ(I) obs: 3 / % possible all: 71.9 |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 2.38→32.4 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.915 / SU B: 18.005 / SU ML: 0.196 / Cross valid method: THROUGHOUT / ESU R: 0.429 / ESU R Free: 0.282 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 29.885 Å2
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.38→32.4 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
|