+Open data
-Basic information
Entry | Database: PDB / ID: 2l17 | ||||||
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Title | An arsenate reductase in the reduced state | ||||||
Components | Arsenate reductase | ||||||
Keywords | OXIDOREDUCTASE / alpha/beta sandwich | ||||||
Function / homology | Function and homology information arsenate reductase (glutathione/glutaredoxin) / arsenate reductase (glutaredoxin) activity / response to arsenic-containing substance / protein-tyrosine-phosphatase / protein tyrosine phosphatase activity Similarity search - Function | ||||||
Biological species | Synechocystis (bacteria) | ||||||
Method | SOLUTION NMR / molecular dynamics | ||||||
Model details | lowest energy, model 1 | ||||||
Authors | Yu, C. / Xia, B. / Jin, C. | ||||||
Citation | Journal: Biomol.Nmr Assign. / Year: 2011 Title: (1)H, (13)C and (15)N resonance assignments of the arsenate reductase from Synechocystis sp. strain PCC 6803 Authors: Yu, C. / Xia, B. / Jin, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 2l17.cif.gz | 777.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb2l17.ent.gz | 653.2 KB | Display | PDB format |
PDBx/mmJSON format | 2l17.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/l1/2l17 ftp://data.pdbj.org/pub/pdb/validation_reports/l1/2l17 | HTTPS FTP |
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-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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NMR ensembles |
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-Components
#1: Protein | Mass: 14739.713 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Synechocystis (bacteria) / Strain: PCC 6803 / Gene: arsC, slr0946 / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3) References: UniProt: P74313, arsenate reductase (glutathione/glutaredoxin) |
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-Experimental details
-Experiment
Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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NMR experiment |
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-Sample preparation
Details |
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Sample |
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Sample conditions | Ionic strength: 0.1 / pH: 7.0 / Pressure: ambient / Temperature: 298 K |
-NMR measurement
NMR spectrometer |
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-Processing
NMR software |
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Refinement | Method: molecular dynamics / Software ordinal: 1 | ||||||||||||||||||
NMR representative | Selection criteria: lowest energy | ||||||||||||||||||
NMR ensemble | Conformer selection criteria: structures with the lowest energy Conformers calculated total number: 200 / Conformers submitted total number: 20 / Representative conformer: 1 |