[English] 日本語
Yorodumi- PDB-3hch: Structure of the C-terminal domain (MsrB) of Neisseria meningitid... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3hch | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of the C-terminal domain (MsrB) of Neisseria meningitidis PilB (complex with substrate) | ||||||
Components | Peptide methionine sulfoxide reductase msrA/msrB | ||||||
Keywords | OXIDOREDUCTASE / PilB / Methionine sulfoxide reductase B / complex with substrate / Disulfide bond / Electron transport / Multifunctional enzyme / Redox-active center / Transport | ||||||
Function / homology | Function and homology information L-methionine:thioredoxin-disulfide S-oxidoreductase activity / peptide-methionine (R)-S-oxide reductase / peptide-methionine (R)-S-oxide reductase activity / peptide-methionine (S)-S-oxide reductase / peptide-methionine (S)-S-oxide reductase activity / protein repair / protein modification process / response to oxidative stress / cytoplasm Similarity search - Function | ||||||
Biological species | Neisseria meningitidis serogroup A (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 2.1 Å | ||||||
Authors | Ranaivoson, F.M. / Kauffmann, B. / Favier, F. | ||||||
Citation | Journal: J.Mol.Biol. / Year: 2009 Title: Methionine sulfoxide reductase B displays a high level of flexibility. Authors: Ranaivoson, F.M. / Neiers, F. / Kauffmann, B. / Boschi-Muller, S. / Branlant, G. / Favier, F. | ||||||
History |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 3hch.cif.gz | 81.4 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb3hch.ent.gz | 61.6 KB | Display | PDB format |
PDBx/mmJSON format | 3hch.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hc/3hch ftp://data.pdbj.org/pub/pdb/validation_reports/hc/3hch | HTTPS FTP |
---|
-Related structure data
Related structure data | 3hcgSC 3hciC 3hcjC S: Starting model for refinement C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 |
| ||||||||
Unit cell |
|
-Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 16366.038 Da / Num. of mol.: 2 / Fragment: MsrB domain (UNP residues 377-522) / Mutation: C440S, C495S Source method: isolated from a genetically manipulated source Source: (gene. exp.) Neisseria meningitidis serogroup A (bacteria) Strain: Z2491 / Gene: msrAB, NMA0290, pilB / Plasmid: pSKPILBMsrB / Production host: Escherichia coli (E. coli) / Strain (production host): BE002 References: UniProt: Q9JWM8, peptide-methionine (R)-S-oxide reductase |
---|
-Non-polymers , 5 types, 176 molecules
#2: Chemical | #3: Chemical | ChemComp-CIT / | #4: Chemical | ChemComp-P6G / #5: Chemical | ChemComp-TRS / | #6: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 4.73 Å3/Da / Density % sol: 73.99 % |
---|---|
Crystal grow | Temperature: 293 K / Method: microbatch under oil / pH: 8.5 Details: 30 % PEG 400, 0.1M TRIS HCl pH 8.5, 0.2M Na Citrate, 0.05M TRIS HCl pH 8, microbatch under oil, temperature 293K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934 Å |
Detector | Type: ADSC QUANTUM 210 / Detector: CCD / Date: Oct 1, 2004 |
Radiation | Monochromator: Diamond (111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 2.1→50 Å / Num. all: 37520 / Num. obs: 37516 / % possible obs: 100 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 32.9 % / Rsym value: 0.075 / Net I/σ(I): 28.1 |
Reflection shell | Resolution: 2.1→2.18 Å / Mean I/σ(I) obs: 3 / Rsym value: 0.428 / % possible all: 100 |
-Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Starting model: 3HCG Resolution: 2.1→14.83 Å / Cor.coef. Fo:Fc: 0.946 / Cor.coef. Fo:Fc free: 0.929 / Occupancy max: 1 / Occupancy min: 0.4 / SU B: 3.086 / SU ML: 0.084 / Cross valid method: THROUGHOUT / ESU R: 0.139 / ESU R Free: 0.133 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 101.17 Å2 / Biso mean: 31.686 Å2 / Biso min: 7.56 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.1→14.83 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Resolution: 2.104→2.157 Å / Total num. of bins used: 20
|