+Open data
-Basic information
Entry | Database: PDB / ID: 5c6p | ||||||
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Title | protein C | ||||||
Components |
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Keywords | TRANSPORT PROTEIN / protein | ||||||
Function / homology | Function and homology information cell-substrate junction assembly / antiporter activity / proteoglycan binding / extracellular matrix structural constituent / xenobiotic transmembrane transporter activity / monoatomic ion transport / cell-matrix adhesion / integrin binding / plasma membrane Similarity search - Function | ||||||
Biological species | Neisseria gonorrhoeae (bacteria) Escherichia coli (E. coli) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 3 Å | ||||||
Authors | Lu, M. | ||||||
Funding support | United States, 1items
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Citation | Journal: Nat Commun / Year: 2015 Title: Structural basis for the blockade of MATE multidrug efflux pumps. Authors: Radchenko, M. / Symersky, J. / Nie, R. / Lu, M. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5c6p.cif.gz | 232.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5c6p.ent.gz | 187.4 KB | Display | PDB format |
PDBx/mmJSON format | 5c6p.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5c6p_validation.pdf.gz | 756.8 KB | Display | wwPDB validaton report |
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Full document | 5c6p_full_validation.pdf.gz | 837.3 KB | Display | |
Data in XML | 5c6p_validation.xml.gz | 24.6 KB | Display | |
Data in CIF | 5c6p_validation.cif.gz | 34.6 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/c6/5c6p ftp://data.pdbj.org/pub/pdb/validation_reports/c6/5c6p | 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: 49717.574 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090) (bacteria) Strain: ATCC 700825 / FA 1090 / Gene: NGO0395 / Production host: Escherichia coli (E. coli) / References: UniProt: Q5F9J8 |
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#2: Protein | Mass: 10916.989 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Escherichia coli (E. coli) / Production host: Escherichia coli (E. coli) / References: UniProt: M1E1G6 |
#3: Chemical | ChemComp-4YH / ( |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION |
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-Sample preparation
Crystal | Density Matthews: 7.45 Å3/Da / Density % sol: 83.48 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / Details: PEG400 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-ID / Wavelength: 1 Å |
Detector | Type: MAR CCD 165 mm / Detector: CCD / Date: Jul 1, 2013 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3→100 Å / Num. obs: 33124 / % possible obs: 91 % / Redundancy: 6 % / Net I/σ(I): 20 |
-Processing
Software |
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Refinement | Resolution: 3→20 Å / Cross valid method: FREE R-VALUE
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Refinement step | Cycle: LAST / Resolution: 3→20 Å
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