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Open data
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Basic information
Entry | Database: PDB / ID: 4aa7 | ||||||
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Title | E.coli GlmU in complex with an antibacterial inhibitor | ||||||
![]() | BIFUNCTIONAL PROTEIN GLMU | ||||||
![]() | TRANSFERASE / ACETYL TRANSFERASE / TRANSFERASE-INHIBITOR COMPLEX | ||||||
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 | ![]() ![]() | ||||||
![]() | Otterbein, L. / Breed, J. / Ogg, D.J. | ||||||
![]() | ![]() Title: Inhibitors of Acetyltransferase Domain of N-Acetylglucosamine-1-Phosphate-Uridyltransferase/ Glucosamine-1-Phosphate-Acetyltransferase (Glmu). Part 1: Hit to Lead Evaluation of a Novel Arylsulfonamide Series. Authors: Green, O.M. / McKenzie, A.R. / Shapiro, A.B. / Otterbein, L. / Ni, H. / Patten, A. / Stokes, S. / Albert, R. / Kawatkar, S. / Breed, J. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 183.4 KB | Display | ![]() |
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PDB format | ![]() | 144.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.1 MB | Display | ![]() |
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Full document | ![]() | 1.1 MB | Display | |
Data in XML | ![]() | 23 KB | Display | |
Data in CIF | ![]() | 33.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 4aawC ![]() 4ac3C ![]() 3twdS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Components on special symmetry positions |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Components
#1: Protein | Mass: 24722.160 Da / Num. of mol.: 2 / Fragment: RESIDUES 227-456 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() References: UniProt: P0ACC7, glucosamine-1-phosphate N-acetyltransferase, UDP-N-acetylglucosamine diphosphorylase #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | Nonpolymer details | R82: N-2,4-DIMETHOXY-5-(2-METHYLINDO | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.78 Å3/Da / Density % sol: 55.83 % / Description: NONE |
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Crystal grow | Method: vapor diffusion, hanging drop / pH: 5.5 Details: 19-22% (W/V) PEG3350, 100MM PCTP PH 5.5 AND 400MM AMMONIUM SULFATE, VAPOR DIFFUSION, HANGING DROP |
-Data collection
Diffraction | Mean temperature: 287 K |
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Diffraction source | Source: ![]() |
Detector | Type: RIGAKU CCD / Detector: CCD / Date: Oct 18, 2005 / Details: RIGAKU VARIMAX HF |
Radiation | Monochromator: NI FILTER / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2→40.36 Å / Num. obs: 33180 / % possible obs: 95 % / Observed criterion σ(I): 2 / Redundancy: 3 % / Rmerge(I) obs: 0.11 / Net I/σ(I): 9 |
Reflection shell | Resolution: 2→2.11 Å / Redundancy: 1.7 % / Rmerge(I) obs: 0.46 / Mean I/σ(I) obs: 2.5 / % possible all: 82 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 3TWD Resolution: 2→40.36 Å / Cor.coef. Fo:Fc: 0.951 / Cor.coef. Fo:Fc free: 0.921 / SU B: 6.847 / SU ML: 0.101 / Cross valid method: THROUGHOUT / ESU R: 0.174 / ESU R Free: 0.157 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. U VALUES WITH TLS ADDED
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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: 16.523 Å2
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Refinement step | Cycle: LAST / Resolution: 2→40.36 Å
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Refine LS restraints |
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