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Yorodumi- PDB-3a1c: crystal structure of the P- and N-domains of CopA, a copper-trans... -
+Open data
-Basic information
Entry | Database: PDB / ID: 3a1c | ||||||
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Title | crystal structure of the P- and N-domains of CopA, a copper-transporting P-type ATPase, bound with AMPPCP-Mg | ||||||
Components | Probable copper-exporting P-type ATPase A | ||||||
Keywords | HYDROLASE / P-type ATPase / ATP-binding / Cell membrane / Copper transport / Ion transport / Magnesium / Membrane / Metal-binding / Nucleotide-binding / Phosphoprotein / Transmembrane / Transport | ||||||
Function / homology | Function and homology information P-type monovalent copper transporter activity / P-type Cu+ transporter / copper ion binding / ATP hydrolysis activity / ATP binding / identical protein binding / plasma membrane Similarity search - Function | ||||||
Biological species | Archaeoglobus fulgidus (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.85 Å | ||||||
Authors | Tsuda, T. / Toyoshima, C. | ||||||
Citation | Journal: Embo J. / Year: 2009 Title: Nucleotide recognition by CopA, a Cu+-transporting P-type ATPase. Authors: Tsuda, T. / Toyoshima, C. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 3a1c.cif.gz | 126.5 KB | Display | PDBx/mmCIF format |
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PDB format | pdb3a1c.ent.gz | 97.3 KB | Display | PDB format |
PDBx/mmJSON format | 3a1c.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/a1/3a1c ftp://data.pdbj.org/pub/pdb/validation_reports/a1/3a1c | HTTPS FTP |
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-Related structure data
Related structure data | 3a1dC 3a1eC 2b8eS C: citing same article (ref.) S: Starting model for refinement |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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Details | The author states that a functinal unit is unknown about this protein and would like to change DIMERIC to UNKNOWN in REMARK 350. |
-Components
#1: Protein | Mass: 30781.383 Da / Num. of mol.: 2 / Fragment: residues 387-673 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Archaeoglobus fulgidus (archaea) / Gene: copA, pacS, AF_0473 / Plasmid: pBAD / Production host: Escherichia coli (E. coli) References: UniProt: O29777, Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to catalyse transmembrane movement of substances #2: Chemical | #3: Chemical | ChemComp-MG / | #4: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 2 |
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-Sample preparation
Crystal | Density Matthews: 3.21 Å3/Da / Density % sol: 61.68 % |
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Crystal grow | Temperature: 283 K / Method: vapor diffusion, hanging drop / pH: 5.5 Details: 5% PEG 6000, 1.5M NaCl, 0.1M MES, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 283K |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL41XU / Wavelength: 0.9 Å |
Detector | Type: ADSC QUANTUM 315 / Detector: CCD / Date: Sep 24, 2007 |
Radiation | Monochromator: rotated-inclined double-crystal / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 1.85→20 Å / Num. obs: 65461 / % possible obs: 99.6 % / Redundancy: 6.2 % / Biso Wilson estimate: 44.9 Å2 / Rmerge(I) obs: 0.081 / Net I/σ(I): 33.7 |
Reflection shell | Resolution: 1.85→1.9 Å / Redundancy: 6.2 % / Rmerge(I) obs: 0.291 / Mean I/σ(I) obs: 2.8 / % possible all: 99.1 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 2B8E Resolution: 1.85→20 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.952 / SU B: 4.99 / SU ML: 0.08 / TLS residual ADP flag: LIKELY RESIDUAL / Cross valid method: THROUGHOUT / ESU R: 0.115 / ESU R Free: 0.112 / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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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: 44.895 Å2
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Refinement step | Cycle: LAST / Resolution: 1.85→20 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 1.85→1.898 Å / Total num. of bins used: 20
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Refinement TLS params. | Method: refined / Refine-ID: X-RAY DIFFRACTION
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Refinement TLS group |
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