+Open data
-Basic information
Entry | Database: PDB / ID: 1mbb | ||||||
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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 division / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2.3 Å | ||||||
Authors | Benson, T.E. / Lees, W.J. / Walsh, C.T. / Hogle, J.M. | ||||||
Citation | Journal: Biochemistry / Year: 1996 Title: (E)-enolbutyryl-UDP-N-acetylglucosamine as a mechanistic probe of UDP-N-acetylenolpyruvylglucosamine reductase (MurB). Authors: Lees, W.J. / Benson, T.E. / Hogle, J.M. / Walsh, C.T. #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 | 1mbb.cif.gz | 84.8 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1mbb.ent.gz | 62.8 KB | Display | PDB format |
PDBx/mmJSON format | 1mbb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1mbb_validation.pdf.gz | 544.1 KB | Display | wwPDB validaton report |
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Full document | 1mbb_full_validation.pdf.gz | 556.6 KB | Display | |
Data in XML | 1mbb_validation.xml.gz | 10.4 KB | Display | |
Data in CIF | 1mbb_validation.cif.gz | 15.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/mb/1mbb ftp://data.pdbj.org/pub/pdb/validation_reports/mb/1mbb | HTTPS FTP |
-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: (E)-ENOLBUTRYRL-UDP-N-ACETYLGLUCOSAMINE, 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-EEB / |
#3: Chemical | ChemComp-FAD / |
#4: Water | ChemComp-HOH / |
Compound details | THE SECONDARY STRUCTURE ASSIGNMENT IN THIS PDB ENTRY REFLECTS THE RESULTS OF AN AUTOMATED PROCEDURE. ...THE SECONDARY STRUCTURE ASSIGNMENT |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 2.18 Å3/Da / Density % sol: 43.54 % | |||||||||||||||||||||||||
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Crystal grow | *PLUS Temperature: 25 ℃ / pH: 8 / Method: vapor diffusion, hanging drop | |||||||||||||||||||||||||
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: 2.3→12 Å / Num. obs: 14935 / % possible obs: 94.9 % |
Reflection | *PLUS Num. measured all: 52502 / Rmerge(I) obs: 0.072 |
-Processing
Software |
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Refinement | Resolution: 2.3→12 Å / σ(F): 0
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Refinement step | Cycle: LAST / Resolution: 2.3→12 Å
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Refine LS restraints |
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