- PDB-5f0w: Crystal structure of human copper homeostatic proteins atox1 -
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Open data
ID or keywords:
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Basic information
Entry
Database: PDB / ID: 5f0w
Title
Crystal structure of human copper homeostatic proteins atox1
Components
Copper transport protein ATOX1
Keywords
METAL BINDING PROTEIN / copper / homeostatic
Function / homology
Function and homology information
metallochaperone activity / Ion influx/efflux at host-pathogen interface / copper-dependent protein binding / copper chaperone activity / copper ion transport / Detoxification of Reactive Oxygen Species / cuprous ion binding / intracellular copper ion homeostasis / response to oxidative stress / copper ion binding / cytosol Similarity search - Function
A: Copper transport protein ATOX1 B: Copper transport protein ATOX1 C: Copper transport protein ATOX1 D: Copper transport protein ATOX1 hetero molecules
Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray
Radiation wavelength
Wavelength: 1.5419 Å / Relative weight: 1
Reflection
Resolution: 2.7→50 Å / Num. obs: 10336 / % possible obs: 90.2 % / Redundancy: 6.2 % / Net I/σ(I): 17.776
Reflection shell
Resolution: 2.7→2.75 Å / Redundancy: 6.3 % / Mean I/σ(I) obs: 4.667 / % possible all: 87.4
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Processing
Software
Name
Version
Classification
REFMAC
5.8.0049
refinement
HKL-3000
datareduction
Refinement
Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.7→24.48 Å / Cor.coef. Fo:Fc: 0.899 / Cor.coef. Fo:Fc free: 0.876 / Cross valid method: THROUGHOUT / ESU R: 0.736 / ESU R Free: 0.362 Stereochemistry target values: MAXIMUM LIKELIHOOD WITH PHASES Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
Rfactor
Num. reflection
% reflection
Selection details
Rfree
0.28935
487
4.5 %
RANDOM
Rwork
0.261
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obs
0.26235
10336
94.54 %
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Solvent computation
Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å / Solvent model: MASK