+Open data
-Basic information
Entry | Database: PDB / ID: 1fee | |||||||||
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Title | CRYSTAL STRUCTURE OF COPPER-HAH1 | |||||||||
Components | COPPER TRANSPORT PROTEIN ATOX1 | |||||||||
Keywords | TRANSPORT PROTEIN / beta-alpha-beta-beta-alpha-beta | |||||||||
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 | |||||||||
Biological species | Homo sapiens (human) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.8 Å | |||||||||
Authors | Wernimont, A.K. / Huffman, D.L. / Lamb, A.L. / O'Halloran, T.V. / Rosenzweig, A.C. | |||||||||
Citation | Journal: Nat.Struct.Biol. / Year: 2000 Title: Structural basis for copper transfer by the metallochaperone for the Menkes/Wilson disease proteins. Authors: Wernimont, A.K. / Huffman, D.L. / Lamb, A.L. / O'Halloran, T.V. / Rosenzweig, A.C. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1fee.cif.gz | 42.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1fee.ent.gz | 29.2 KB | Display | PDB format |
PDBx/mmJSON format | 1fee.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1fee_validation.pdf.gz | 456.1 KB | Display | wwPDB validaton report |
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Full document | 1fee_full_validation.pdf.gz | 457.4 KB | Display | |
Data in XML | 1fee_validation.xml.gz | 4.5 KB | Display | |
Data in CIF | 1fee_validation.cif.gz | 7.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/fe/1fee ftp://data.pdbj.org/pub/pdb/validation_reports/fe/1fee | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 7412.646 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Organ: LIVER / Plasmid: PMAGDA / Production host: Escherichia coli (E. coli) / References: UniProt: O00244 #2: Polysaccharide | beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose / sucrose | #3: Chemical | ChemComp-CU1 / | #4: Chemical | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 3.26 Å3/Da / Density % sol: 62.23 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 6.5 Details: Strictly anaerobic. MES buffer, lithium sulfate, and dithiothreitol, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 113 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 5ID-B / Wavelength: 1.37 |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Mar 14, 2000 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.37 Å / Relative weight: 1 |
Reflection | Resolution: 1.8→50 Å / Num. all: 428425 / Num. obs: 21017 / % possible obs: 99.7 % / Observed criterion σ(F): 2 / Observed criterion σ(I): 2 / Redundancy: 5 % / Biso Wilson estimate: 20.7 Å2 / Rmerge(I) obs: 0.081 / Net I/σ(I): 3.3 |
Reflection shell | Resolution: 1.8→1.85 Å / Redundancy: 4 % / Rmerge(I) obs: 0.27 / % possible all: 97 |
Reflection | *PLUS Lowest resolution: 50 Å / Num. measured all: 428425 |
Reflection shell | *PLUS % possible obs: 99.7 % / Rmerge(I) obs: 0.275 / Mean I/σ(I) obs: 2.3 |
-Processing
Software |
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Refinement | Resolution: 1.8→50 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Refinement step | Cycle: LAST / Resolution: 1.8→50 Å
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Refine LS restraints |
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Software | *PLUS Name: CNS / Version: 0.9 / Classification: refinement | |||||||||||||||||||||||||
Refinement | *PLUS Lowest resolution: 50 Å / σ(F): 0 / % reflection Rfree: 10 % | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 23.6 Å2 | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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