+Open data
-Basic information
Entry | Database: PDB / ID: 6pce | ||||||||||||
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Title | Human Coa6 | ||||||||||||
Components | Cytochrome c oxidase assembly factor 6 homolog | ||||||||||||
Keywords | METAL BINDING PROTEIN / Coa6 copper Cytochrome c oxidase mitochondria structure | ||||||||||||
Function / homology | Function and homology information plasma membrane ATP synthesis coupled electron transport / respiratory chain complex IV assembly / respiratory chain complex IV / Mitochondrial protein import / mitochondrial ATP synthesis coupled electron transport / mitochondrial intermembrane space / copper ion binding / mitochondrion / RNA binding / nucleoplasm / plasma membrane Similarity search - Function | ||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / SAD / Resolution: 1.65 Å | ||||||||||||
Authors | Maher, M.J. / Maghool, S. | ||||||||||||
Funding support | Australia, 3items
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Citation | Journal: Life Sci Alliance / Year: 2019 Title: Structural and functional characterization of the mitochondrial complex IV assembly factor Coa6. Authors: Maghool, S. / Cooray, N.D.G. / Stroud, D.A. / Aragao, D. / Ryan, M.T. / Maher, M.J. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 6pce.cif.gz | 53 KB | Display | PDBx/mmCIF format |
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PDB format | pdb6pce.ent.gz | 41.1 KB | Display | PDB format |
PDBx/mmJSON format | 6pce.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 6pce_validation.pdf.gz | 437.1 KB | Display | wwPDB validaton report |
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Full document | 6pce_full_validation.pdf.gz | 438.1 KB | Display | |
Data in XML | 6pce_validation.xml.gz | 7.6 KB | Display | |
Data in CIF | 6pce_validation.cif.gz | 9.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/pc/6pce ftp://data.pdbj.org/pub/pdb/validation_reports/pc/6pce | 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: 8550.630 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: COA6, C1orf31 / Production host: Escherichia coli (E. coli) / References: UniProt: Q5JTJ3 #2: Chemical | ChemComp-SO4 / | #3: Water | ChemComp-HOH / | Has ligand of interest | N | |
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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: 2.04 Å3/Da / Density % sol: 39.69 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, hanging drop / Details: 0.1 M HEPES, pH 7.6, 29% (w/v) PEG 3350 |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: SYNCHROTRON / Site: Australian Synchrotron / Beamline: MX2 / Wavelength: 0.9918 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 1, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9918 Å / Relative weight: 1 |
Reflection | Resolution: 1.65→50 Å / Num. obs: 16393 / % possible obs: 99.8 % / Redundancy: 4.9 % / Net I/σ(I): 29.9 |
Reflection shell | Resolution: 1.65→1.71 Å / Num. unique obs: 1602 |
-Processing
Software |
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Refinement | Method to determine structure: SAD / Resolution: 1.65→43.55 Å / Cor.coef. Fo:Fc: 0.964 / Cor.coef. Fo:Fc free: 0.946 / SU B: 2.764 / SU ML: 0.076 / Cross valid method: THROUGHOUT / ESU R: 0.111 / ESU R Free: 0.111 / 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 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 29.561 Å2
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Refinement step | Cycle: 1 / Resolution: 1.65→43.55 Å
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Refine LS restraints |
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