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Yorodumi- PDB-1nhr: AN L40C MUTATION CONVERTS THE CYSTEINE-SULFENIC ACID REDOX CENTRE... -
+Open data
-Basic information
Entry | Database: PDB / ID: 1nhr | ||||||
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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: 2.1 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 | 1nhr.cif.gz | 106.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1nhr.ent.gz | 81.3 KB | Display | PDB format |
PDBx/mmJSON format | 1nhr.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1nhr_validation.pdf.gz | 475.2 KB | Display | wwPDB validaton report |
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Full document | 1nhr_full_validation.pdf.gz | 482.9 KB | Display | |
Data in XML | 1nhr_validation.xml.gz | 10.8 KB | Display | |
Data in CIF | 1nhr_validation.cif.gz | 17.4 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/nh/1nhr ftp://data.pdbj.org/pub/pdb/validation_reports/nh/1nhr | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 49593.215 Da / Num. of mol.: 1 / Mutation: L40C 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 | #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: 3.84 Å3/Da / Density % sol: 67.94 % | ||||||||||||||||||||||||||||||||||||||||
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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: 44912 / % possible obs: 91.7 % / Observed criterion σ(I): 0 |
Reflection | *PLUS Highest resolution: 2.1 Å / Rmerge(I) obs: 0.057 |
Reflection shell | *PLUS Highest resolution: 2 Å / Lowest resolution: 2.13 Å / % possible obs: 80 % |
-Processing
Software |
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Refinement | Resolution: 2.1→8 Å / σ(F): 2 /
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Displacement parameters | Biso mean: 21.9 Å2 | |||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→8 Å
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Refinement | *PLUS Rfactor obs: 0.17 / Rfactor Rwork: 0.17 | |||||||||||||||
Solvent computation | *PLUS | |||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||
Refine LS restraints | *PLUS
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