+Open data
-Basic information
Entry | Database: PDB / ID: 2lqo | ||||||
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Title | Mrx1 reduced | ||||||
Components | Putative glutaredoxin Rv3198.1/MT3292 | ||||||
Keywords | OXIDOREDUCTASE / Trx fold | ||||||
Function / homology | Function and homology information : / Oxidoreductases / cell redox homeostasis / electron transfer activity / oxidoreductase activity Similarity search - Function | ||||||
Biological species | Mycobacterium tuberculosis (bacteria) | ||||||
Method | SOLUTION NMR / simulated annealing | ||||||
Model details | closest to the average, model 1 | ||||||
Authors | Buts, L. / Van Laer, K. / Messens, J. | ||||||
Citation | Journal: Mol.Microbiol. / Year: 2012 Title: Mycoredoxin-1 is one of the missing links in the oxidative stress defence mechanism of Mycobacteria. Authors: Van Laer, K. / Buts, L. / Foloppe, N. / Vertommen, D. / Van Belle, K. / Wahni, K. / Roos, G. / Nilsson, L. / Mateos, L.M. / Rawat, M. / van Nuland, N.A. / Messens, J. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2lqo.cif.gz | 511.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2lqo.ent.gz | 428.1 KB | Display | PDB format |
PDBx/mmJSON format | 2lqo.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 2lqo_validation.pdf.gz | 538.6 KB | Display | wwPDB validaton report |
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Full document | 2lqo_full_validation.pdf.gz | 1.1 MB | Display | |
Data in XML | 2lqo_validation.xml.gz | 137.1 KB | Display | |
Data in CIF | 2lqo_validation.cif.gz | 103 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lq/2lqo ftp://data.pdbj.org/pub/pdb/validation_reports/lq/2lqo | HTTPS FTP |
-Related structure data
Related structure data | 2lqqC C: citing same article (ref.) |
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Similar structure data | |
Other databases |
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-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 10030.316 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Mycobacterium tuberculosis (bacteria) / Gene: Rv3198.1, MT3292, Rv3198A / Production host: Escherichia coli (E. coli) References: UniProt: Q8VJ51, UniProt: P9WN17*PLUS, Oxidoreductases |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details | Contents: 0.8-1.0 mM [U-99% 13C; U-99% 15N] protein, 90% H2O/10% D2O Solvent system: 90% H2O/10% D2O |
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Sample | Units: mM / Component: entity-1 / Isotopic labeling: [U-99% 13C; U-99% 15N] / Conc. range: 0.8-1.0 |
Sample conditions | Ionic strength: 0 / pH: 6.6 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: simulated annealing / Software ordinal: 1 | |||||||||||||||||||||
NMR constraints | NOE constraints total: 1872 / NOE intraresidue total count: 394 / NOE long range total count: 602 / Protein phi angle constraints total count: 74 / Protein psi angle constraints total count: 73 | |||||||||||||||||||||
NMR representative | Selection criteria: closest to the average | |||||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 100 / Conformers submitted total number: 20 |