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Yorodumi- PDB-1nhs: AN L40C MUTATION CONVERTS THE CYSTEINE-SULFENIC ACID REDOX CENTRE... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1nhs | ||||||
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Title | AN L40C MUTATION CONVERTS THE CYSTEINE-SULFENIC ACID REDOX CENTRE IN ENTEROCOCCAL NADH PEROXIDASE TO A DISULFIDE | ||||||
Components | NADH PEROXIDASE | ||||||
Keywords | OXIDOREDUCTASE (H2O2(A)) | ||||||
Function / homology | Function and homology information NADH peroxidase / NADH peroxidase activity / flavin adenine dinucleotide binding Similarity search - Function | ||||||
Biological species | Enterococcus faecalis (bacteria) | ||||||
Method | X-RAY DIFFRACTION / Resolution: 2 Å | ||||||
Authors | Mande, S.S. / Claiborne, A. / Hol, W.G.J. | ||||||
Citation | Journal: Biochemistry / Year: 1995 Title: An L40C mutation converts the cysteine-sulfenic acid redox center in enterococcal NADH peroxidase to a disulfide. Authors: Miller, H. / Mande, S.S. / Parsonage, D. / Sarfaty, S.H. / Hol, W.G. / Claiborne, A. #1: Journal: J.Mol.Biol. / Year: 1991 Title: Structure of Nadh Peroxidase from Streptococcus Faecalis 10C1 Refined at 2.16 Angstroms Authors: Stehle, T. / Ahmed, S.A. / Claiborne, A. / Schulz, G.E. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1nhs.cif.gz | 102 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1nhs.ent.gz | 82.7 KB | Display | PDB format |
PDBx/mmJSON format | 1nhs.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nh/1nhs ftp://data.pdbj.org/pub/pdb/validation_reports/nh/1nhs | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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2 |
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Unit cell |
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Details | NADH PEROXIDASE IS A TETRAMER CONSISTING OF FOUR IDENTICAL SUBUNITS. THE SUBUNITS ARE RELATED THROUGH CRYSTALLOGRAPHIC SYMMETRY OPERATIONS. |
-Components
#1: Protein | Mass: 49667.289 Da / Num. of mol.: 1 / Mutation: S41C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Enterococcus faecalis (bacteria) / References: UniProt: P37062, NADH peroxidase |
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#2: Chemical | ChemComp-SO4 / |
#3: Chemical | ChemComp-FAD / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 3.83 Å3/Da / Density % sol: 67.85 % | ||||||||||||||||||||||||||||||||||||||||
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Crystal grow | *PLUS pH: 7 / 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 | Num. obs: 51780 / % possible obs: 85.9 % / Observed criterion σ(I): 0 |
Reflection | *PLUS Highest resolution: 2 Å / Rmerge(I) obs: 0.054 |
Reflection shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.04 Å / % possible obs: 69.7 % |
-Processing
Software |
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Refinement | Resolution: 2→8 Å / σ(F): 2 /
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Displacement parameters | Biso mean: 19.8 Å2 | |||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2→8 Å
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Refine LS restraints | *PLUS
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