+Open data
-Basic information
Entry | Database: PDB / ID: 1mbt | ||||||
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Title | OXIDOREDUCTASE | ||||||
Components | URIDINE DIPHOSPHO-N-ACETYLENOLPYRUVYLGLUCOSAMINE REDUCTASE | ||||||
Keywords | OXIDOREDUCTASE / FLAVOENZYME | ||||||
Function / homology | Function and homology information 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 cycle / cell division / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 3 Å | ||||||
Authors | Benson, T.E. / Walsh, C.T. / Hogle, J.M. | ||||||
Citation | Journal: Structure / Year: 1996 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: Journal: Nat.Struct.Biol. / Year: 1995 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: Journal: Protein Sci. / Year: 1994 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: Journal: Biochemistry / Year: 1993 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: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1mbt.cif.gz | 73.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mbt.ent.gz | 55 KB | Display | PDB format |
PDBx/mmJSON format | 1mbt.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mb/1mbt ftp://data.pdbj.org/pub/pdb/validation_reports/mb/1mbt | HTTPS FTP |
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-Related structure data
Similar structure data |
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-Links
-Assembly
Deposited unit |
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1 |
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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) Escherichia coli (E. coli) / Strain: AB1157 (ATCC) / References: UniProt: P08373, EC: 1.1.1.158 |
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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: X-RAY DIFFRACTION |
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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 |
-Processing
Software |
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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 |