- PDB-6etb: Aerobic S262Y mutation of E. coli FLRD core -
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Open data
ID or keywords:
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Basic information
Entry
Database: PDB / ID: 6etb
Title
Aerobic S262Y mutation of E. coli FLRD core
Components
Anaerobic nitric oxide reductase flavorubredoxin
Keywords
OXIDOREDUCTASE / Flavorubredoxin / flavodiiron protein / diiron center / nitric oxide reductase
Function / homology
Function and homology information
nitric oxide reductase activity / nitric oxide catabolic process / oxidoreductase activity, acting on other nitrogenous compounds as donors / response to nitric oxide / FMN binding / electron transfer activity / iron ion binding / protein-containing complex / identical protein binding / cytoplasm Similarity search - Function
Mass: 18.015 Da / Num. of mol.: 782 / Source method: isolated from a natural source / Formula: H2O
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Experimental details
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Experiment
Experiment
Method: X-RAY DIFFRACTION / Number of used crystals: 1
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Sample preparation
Crystal
Density Matthews: 2.28 Å3/Da / Density % sol: 45.9 %
Crystal grow
Temperature: 293.15 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: 1.0 UL OF PROTEIN AT 15 MG/ML WITH 2.0 UL OF CRYSTALLIZATION SOLUTION (0.1 M SODIUM CITRATE PH 5.6, 20% (W/V) PEG 4000 AND 20% (V/V) 2-PROPANOL)
Resolution: 1.905→75.758 Å / SU ML: 0.19 / Cross valid method: FREE R-VALUE / σ(F): 16.64 / Phase error: 19.98 Details: The refinement of S262Y mutation from E. coli FLRD core converged to Rwork and Rfree of 0.2174 and 0.2348, respectively, using a Rfree test set size of 1.51% (799 reflections). The final ...Details: The refinement of S262Y mutation from E. coli FLRD core converged to Rwork and Rfree of 0.2174 and 0.2348, respectively, using a Rfree test set size of 1.51% (799 reflections). The final model then was refined versus the full data, resulting a final R value of 0.1998.