+Open data
-Basic information
Entry | Database: PDB / ID: 4a48 | ||||||
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Title | Crosstalk between Cu(I) and Zn(II) homeostasis | ||||||
Components | PROBABLE COPPER-TRANSPORTING ATPASE PACS | ||||||
Keywords | TRANSPORT PROTEIN / COPPER HOMEOSTASIS / ZINC HOMEOSTASIS / ATX1 / METAL-TRANSPORTING ATPASES | ||||||
Function / homology | Function and homology information P-type divalent copper transporter activity / P-type monovalent copper transporter activity / P-type Cu+ transporter / copper ion import / copper ion homeostasis / copper ion binding / ATP hydrolysis activity / ATP binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | SYNECHOCYSTIS (bacteria) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.4 Å | ||||||
Authors | Badarau, A. / Basle, A. / Firbank, S.J. / Denninson, C. | ||||||
Citation | Journal: Biochemistry / Year: 2013 Title: Investigating the Role of Zinc and Copper Binding Motifs of Trafficking Sites in the Cyanobacterium Synechocystis Pcc 6803. Authors: Badarau, A. / Basle, A. / Firbank, S.J. / Dennison, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 4a48.cif.gz | 70.3 KB | Display | PDBx/mmCIF format |
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PDB format | pdb4a48.ent.gz | 51.5 KB | Display | PDB format |
PDBx/mmJSON format | 4a48.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 4a48_validation.pdf.gz | 425.7 KB | Display | wwPDB validaton report |
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Full document | 4a48_full_validation.pdf.gz | 426.1 KB | Display | |
Data in XML | 4a48_validation.xml.gz | 8.4 KB | Display | |
Data in CIF | 4a48_validation.cif.gz | 11.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a4/4a48 ftp://data.pdbj.org/pub/pdb/validation_reports/a4/4a48 | HTTPS FTP |
-Related structure data
Related structure data | 4a47C 4a4jC 2xmwS S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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2 |
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Unit cell |
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-Components
#1: Protein | Mass: 7397.318 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-70 Source method: isolated from a genetically manipulated source Source: (gene. exp.) SYNECHOCYSTIS (bacteria) / Strain: PCC 6803 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): BL21(DE3) / References: UniProt: P73241, EC: 3.6.3.54 #2: Chemical | #3: Chemical | #4: 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: 1.8 Å3/Da / Density % sol: 32 % / Description: NONE |
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Crystal grow | Details: 200 MM NAF, 20% (W/V) PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: Diamond / Beamline: I02 / Wavelength: 0.9795 |
Detector | Type: ADSC CCD / Detector: CCD / Date: May 30, 2011 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 1.4→31.59 Å / Num. obs: 18146 / % possible obs: 91.4 % / Observed criterion σ(I): 2 / Redundancy: 4 % / Biso Wilson estimate: 12.1 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 15.3 |
Reflection shell | Resolution: 1.4→1.48 Å / Redundancy: 4 % / Rmerge(I) obs: 0.22 / Mean I/σ(I) obs: 5.1 / % possible all: 86.2 |
-Processing
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2XMW Resolution: 1.4→39.52 Å / Cor.coef. Fo:Fc: 0.971 / Cor.coef. Fo:Fc free: 0.948 / SU B: 2.512 / SU ML: 0.045 / Cross valid method: THROUGHOUT / ESU R: 0.085 / ESU R Free: 0.075 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. U VALUES REFINED INDIVIDUALLY. DISORDERED ATOMS WERE REMOVED
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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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 14.371 Å2
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Refinement step | Cycle: LAST / Resolution: 1.4→39.52 Å
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Refine LS restraints |
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