- PDB-2y3q: 1.55A structure of apo bacterioferritin from E. coli -
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Open data
ID or keywords:
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Basic information
Entry
Database: PDB / ID: 2y3q
Title
1.55A structure of apo bacterioferritin from E. coli
Components
BACTERIOFERRITIN
Keywords
METAL BINDING PROTEIN / REDOX
Function / homology
Function and homology information
ferroxidase / intracellular sequestering of iron ion / ferroxidase activity / ferric iron binding / iron ion transport / oxidoreductase activity / iron ion binding / heme binding / protein homodimerization activity / identical protein binding ...ferroxidase / intracellular sequestering of iron ion / ferroxidase activity / ferric iron binding / iron ion transport / oxidoreductase activity / iron ion binding / heme binding / protein homodimerization activity / identical protein binding / membrane / cytosol Similarity search - Function
Resolution: 1.55→43.23 Å / Cor.coef. Fo:Fc: 0.968 / Cor.coef. Fo:Fc free: 0.956 / SU B: 2.374 / SU ML: 0.039 / Cross valid method: THROUGHOUT / ESU R: 0.077 / ESU R Free: 0.07 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.20007
21922
5 %
RANDOM
Rwork
0.16476
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obs
0.16652
416504
100 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.4 Å / Solvent model: MASK