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- PDB-1uxy: MURB MUTANT WITH SER 229 REPLACED BY ALA, COMPLEX WITH ENOLPYRUVY... -
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Open data
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Basic information
Entry | Database: PDB / ID: 1uxy | ||||||
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Title | MURB MUTANT WITH SER 229 REPLACED BY ALA, COMPLEX WITH ENOLPYRUVYL-UDP-N-ACETYLGLUCOSAMINE | ||||||
![]() | URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / PEPTIDOGLYCAN SYNTHESIS / CELL WALL / CELL DIVISION / NADP / FLAVOPROTEIN / FAD | ||||||
Function / homology | ![]() UDP-N-acetylmuramate dehydrogenase / UDP-N-acetylmuramate dehydrogenase activity / peptidoglycan biosynthetic process / FAD binding / cell wall organization / flavin adenine dinucleotide binding / regulation of cell shape / cell division / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Benson, T.E. / Walsh, C.T. / Hogle, J.M. | ||||||
![]() | ![]() Title: X-ray crystal structures of the S229A mutant and wild-type MurB in the presence of the substrate enolpyruvyl-UDP-N-acetylglucosamine at 1.8-A resolution. Authors: Benson, T.E. / Walsh, C.T. / Hogle, J.M. #1: ![]() Title: Kinetic Characterization of Wild-Type and S229A Mutant Murb: Evidence for the Role of Ser 229 as a General Acid Authors: Benson, T.E. / Walsh, C.T. / Massey, V. #2: ![]() Title: An Enzyme-Substrate Complex Involved in Bacterial Cell Wall Biosynthesis Authors: Benson, T.E. / Filman, D.J. / Walsh, C.T. / Hogle, J.M. #3: ![]() Title: Crystallization and Preliminary X-Ray Crystallographic Studies of Udp-N-Acetyl Enolpyruvylglucosamine Reductase Authors: Benson, T.E. / Walsh, C.T. / Hogle, J.M. #4: ![]() Title: Overexpression, Purification, and Mechanistic Study of Udp-N-Acetylenolpyruvylglucosamine Reductase Authors: Benson, T.E. / Marquardt, J.L. / Marquardt, A.C. / Etzkorn, F.A. / Walsh, C.T. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 87.4 KB | Display | ![]() |
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PDB format | ![]() | 64.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 547 KB | Display | ![]() |
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Full document | ![]() | 556 KB | Display | |
Data in XML | ![]() | 10 KB | Display | |
Data in CIF | ![]() | 15.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 37630.613 Da / Num. of mol.: 1 / Mutation: S229A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() |
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#2: Chemical | ChemComp-FAD / |
#3: Chemical | ChemComp-EPU / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.1 Å3/Da / Density % sol: 41.54 % | ||||||||||||||||||||||||||||||
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Crystal grow | pH: 8 / Details: pH 8.0 | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS Method: vapor diffusion | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction source | Source: ![]() ![]() ![]() |
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Radiation | Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 1.8→20 Å / Num. obs: 29142 / % possible obs: 92.9 % |
Reflection | *PLUS Redundancy: 5.7 % / Rmerge(I) obs: 0.057 |
Reflection shell | *PLUS Highest resolution: 1.8 Å / Lowest resolution: 1.88 Å / % possible obs: 79.6 % / Redundancy: 4.4 % / Num. unique obs: 3066 / Rmerge(I) obs: 0.181 / Mean I/σ(I) obs: 8.13 |
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Processing
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Refinement | Resolution: 1.8→20 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 1.8→20 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS Type: x_improper_angle_deg / Dev ideal: 1.34 |