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Open data
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Basic information
Entry | Database: PDB / ID: 2xmw | ||||||
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Title | PacS, N-terminal domain, from Synechocystis PCC6803 | ||||||
![]() | CATION-TRANSPORTING ATPASE PACS | ||||||
![]() | HYDROLASE / CU(I)-BINDING / TRAFFICKING | ||||||
Function / homology | ![]() P-type divalent copper transporter activity / P-type monovalent copper transporter activity / P-type Cu+ transporter / copper ion export / copper ion import / copper ion homeostasis / intracellular copper ion homeostasis / copper ion binding / ATP hydrolysis activity / ATP binding ...P-type divalent copper transporter activity / P-type monovalent copper transporter activity / P-type Cu+ transporter / copper ion export / copper ion import / copper ion homeostasis / intracellular copper ion homeostasis / copper ion binding / ATP hydrolysis activity / ATP binding / membrane / plasma membrane Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Badarau, A. / Firbank, S.J. / McCarthy, A.A. / Banfield, M.J. / Dennison, C. | ||||||
![]() | ![]() Title: Visualizing the Metal-Binding Versatility of Copper Trafficking Sites . Authors: Badarau, A. / Firbank, S.J. / Mccarthy, A.A. / Banfield, M.J. / Dennison, C. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 25.2 KB | Display | ![]() |
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PDB format | ![]() | 15.3 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 419.3 KB | Display | ![]() |
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Full document | ![]() | 419.3 KB | Display | |
Data in XML | ![]() | 4.8 KB | Display | |
Data in CIF | ![]() | 5.8 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2xmjC ![]() 2xmkC ![]() 2xmmC ![]() 2xmtC ![]() 2xmuC ![]() 2xmvC C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 7653.774 Da / Num. of mol.: 1 / Fragment: N-TERMINAL, COPPER-BINDING DOMAIN, RESIDUES 1-71 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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#2: Chemical | ChemComp-CU1 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.03 Å3/Da / Density % sol: 39.43 % / Description: NONE |
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Crystal grow | pH: 4.6 Details: 40 % (W/V) PEG 300 AND 100 MM CITRATE -PHOSPHATE PH 4.6 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC CCD / Detector: CCD / Date: Sep 15, 2009 / Details: MIRRORS |
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→39.47 Å / Num. obs: 6085 / % possible obs: 100 % / Observed criterion σ(I): 0 / Redundancy: 23.5 % / Rmerge(I) obs: 0.07 / Net I/σ(I): 39 |
Reflection shell | Resolution: 1.8→1.9 Å / Redundancy: 23.9 % / Rmerge(I) obs: 0.42 / Mean I/σ(I) obs: 10.3 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: NONE Resolution: 1.8→51.85 Å / Cor.coef. Fo:Fc: 0.927 / Cor.coef. Fo:Fc free: 0.93 / SU B: 2.233 / SU ML: 0.069 / Cross valid method: THROUGHOUT / ESU R: 0.172 / ESU R Free: 0.146 / Stereochemistry target values: MAXIMUM LIKELIHOOD Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. U VALUES REFINED INDIVIDUALLY.
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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: 23.632 Å2
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Refinement step | Cycle: LAST / Resolution: 1.8→51.85 Å
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Refine LS restraints |
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