+
Open data
-
Basic information
Entry | Database: PDB / ID: 2oi5 | ||||||
---|---|---|---|---|---|---|---|
Title | E. coli GlmU- Complex with UDP-GlcNAc and Acetyl-CoA | ||||||
![]() | Bifunctional protein glmU | ||||||
![]() | TRANSFERASE / LEFT-HANDED BETA HELIX | ||||||
Function / homology | ![]() glucosamine-1-phosphate N-acetyltransferase / glucosamine-1-phosphate N-acetyltransferase activity / UDP-N-acetylglucosamine diphosphorylase / UDP-N-acetylglucosamine diphosphorylase activity / UDP-N-acetylglucosamine biosynthetic process / lipid A biosynthetic process / peptidoglycan biosynthetic process / cell morphogenesis / cell wall organization / regulation of cell shape ...glucosamine-1-phosphate N-acetyltransferase / glucosamine-1-phosphate N-acetyltransferase activity / UDP-N-acetylglucosamine diphosphorylase / UDP-N-acetylglucosamine diphosphorylase activity / UDP-N-acetylglucosamine biosynthetic process / lipid A biosynthetic process / peptidoglycan biosynthetic process / cell morphogenesis / cell wall organization / regulation of cell shape / magnesium ion binding / identical protein binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Olsen, L.R. / Vetting, M.W. / Roderick, S.L. | ||||||
![]() | ![]() Title: Structure of the E. coli bifunctional GlmU acetyltransferase active site with substrates and products. Authors: Olsen, L.R. / Vetting, M.W. / Roderick, S.L. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 203.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 159.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.5 MB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 1.6 MB | Display | |
Data in XML | ![]() | 41.4 KB | Display | |
Data in CIF | ![]() | 60.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2oi6C ![]() 2oi7C ![]() 1hv9S S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| |||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| |||||||||||||||
2 | ![]()
| |||||||||||||||
Unit cell |
| |||||||||||||||
Components on special symmetry positions |
| |||||||||||||||
Details | The biological assembly is trimeric. One trimer is assembled by a crystallographic threefold operation on subunit A. A second trimer is assembled by a crystallographic threefold operation on subunit B. The crystallographic threefold rotation is at (x,y) = (1/3,2/3). |
-
Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 49250.906 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P0ACC7, UDP-N-acetylglucosamine diphosphorylase, glucosamine-1-phosphate N-acetyltransferase |
---|
-Non-polymers , 5 types, 641 molecules ![](data/chem/img/MG.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/ACO.gif)
![](data/chem/img/UD1.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/SO4.gif)
![](data/chem/img/ACO.gif)
![](data/chem/img/UD1.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | ChemComp-MG / #3: Chemical | #4: Chemical | #5: Chemical | #6: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.31 Å3/Da / Density % sol: 62.79 % |
---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.1 Details: Tris, NaCl, DTT, Azide, MgCl2, acetyl-CoA, Glc-1-PO4, UDP-GlcNAc, ammonium sulfate, CoCl2, pH 6.1, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 125 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Feb 2, 2001 / Details: Mirrors |
Radiation | Monochromator: Mirrors / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9465 Å / Relative weight: 1 |
Reflection | Resolution: 2.25→23.87 Å / Num. all: 62537 / Num. obs: 62537 / % possible obs: 96.5 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.3 % / Biso Wilson estimate: 15.6 Å2 / Rmerge(I) obs: 0.057 |
Reflection shell | Resolution: 2.25→2.33 Å / Rmerge(I) obs: 0.239 / % possible all: 91.4 |
-
Processing
Software |
| |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: pdb entry 1HV9 Resolution: 2.25→23.87 Å / Rfactor Rfree error: 0.004 / Data cutoff high absF: 138794.55 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / Stereochemistry target values: Engh & Huber
| |||||||||||||||||||||||||
Solvent computation | Solvent model: FLAT MODEL / Bsol: 48.396 Å2 / ksol: 0.401806 e/Å3 | |||||||||||||||||||||||||
Displacement parameters | Biso mean: 27.3 Å2
| |||||||||||||||||||||||||
Refine analyze |
| |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.25→23.87 Å
| |||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||
LS refinement shell | Resolution: 2.25→2.33 Å / Rfactor Rfree error: 0.019 / Total num. of bins used: 10
| |||||||||||||||||||||||||
Xplor file |
|