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Open data
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Basic information
Entry | Database: PDB / ID: 1mbt | ||||||
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Title | OXIDOREDUCTASE | ||||||
![]() | URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE | ||||||
![]() | OXIDOREDUCTASE / FLAVOENZYME | ||||||
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: The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls. Authors: Benson, T.E. / Walsh, C.T. / Hogle, J.M. #1: ![]() Title: An Enzyme-Substrate Complex Involved in Bacterial Cell Wall Biosynthesis Authors: Benson, T.E. / Filman, D.J. / Walsh, C.T. / Hogle, J.M. #2: ![]() Title: Crystallization and Preliminary X-Ray Crystallographic Studies of Udp-N-Acetyl Enolpyruvylglucosamine Reductase Authors: Benson, T.E. / Walsh, C.T. / Hogle, J.M. #3: ![]() 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 | ![]() | 73.4 KB | Display | ![]() |
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PDB format | ![]() | 55 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 473.4 KB | Display | ![]() |
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Full document | ![]() | 482 KB | Display | |
Data in XML | ![]() | 9.8 KB | Display | |
Data in CIF | ![]() | 13.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar 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: 37891.910 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Details: BOUND FLAVIN-ADENINE DINUCLEOTIDE, PH 8.0 / Source: (natural) ![]() ![]() |
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#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-FAD / |
#4: Water | ChemComp-HOH / |
Compound details | DENSITY. THE SECONDARY STRUCTURE ASSIGNMENT IN THIS PDB ENTRY REFLECTS THE RESULTS OF AN AUTOMATED ...DENSITY. THE SECONDARY STRUCTURE ASSIGNMENT |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.39 Å3/Da / Density % sol: 48.47 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 25 unknown / pH: 8 / Method: unknown | |||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Radiation | Scattering type: x-ray |
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Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 3→12 Å / Num. obs: 7297 / % possible obs: 95.9 % |
Reflection | *PLUS Redundancy: 5 % / Num. measured all: 36458 / Rmerge(I) obs: 0.084 |
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Processing
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Refinement | Resolution: 3→12 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 3→12 Å
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Refine LS restraints |
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Refinement | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 21.6 Å2 |