+Open data
-Basic information
Entry | Database: PDB / ID: 5cfy | |||||||||
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Title | CRYSTAL STRUCTURE OF GLTPH R397A IN COMPLEX WITH NA+ AND L-ASP | |||||||||
Components | 425aa long hypothetical proton glutamate symport protein | |||||||||
Keywords | TRANSPORT PROTEIN / ASPARTATE TRANSPORTER / MEMBRANE PROTEIN | |||||||||
Function / homology | Function and homology information amino acid:sodium symporter activity / L-aspartate transmembrane transport / L-aspartate transmembrane transporter activity / L-aspartate import across plasma membrane / chloride transmembrane transporter activity / protein homotrimerization / chloride transmembrane transport / identical protein binding / metal ion binding / plasma membrane Similarity search - Function | |||||||||
Biological species | Pyrococcus horikoshii (archaea) | |||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.5 Å | |||||||||
Authors | Boudker, O. / Oh, S. | |||||||||
Citation | Journal: Elife / Year: 2014 Title: Coupled ion binding and structural transitions along the transport cycle of glutamate transporters. Authors: Verdon, G. / Oh, S. / Serio, R.N. / Boudker, O. | |||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5cfy.cif.gz | 915.9 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5cfy.ent.gz | 776.8 KB | Display | PDB format |
PDBx/mmJSON format | 5cfy.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5cfy_validation.pdf.gz | 506.4 KB | Display | wwPDB validaton report |
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Full document | 5cfy_full_validation.pdf.gz | 607.5 KB | Display | |
Data in XML | 5cfy_validation.xml.gz | 93.8 KB | Display | |
Data in CIF | 5cfy_validation.cif.gz | 125.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/cf/5cfy ftp://data.pdbj.org/pub/pdb/validation_reports/cf/5cfy | HTTPS FTP |
-Related structure data
Related structure data | 4oyeC 4oyfC 4p19C 4p1aC 4p3jC 4p6hC 2nwxS 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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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments:
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-Components
#1: Protein | Mass: 44820.145 Da / Num. of mol.: 6 / Mutation: D37H, K40H, K132H, K223H, K264H, E368H, R397A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) (archaea) Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3 Gene: PH1295 / Production host: ESCHERICHIA COLI (E. coli) / Strain (production host): DH10B / References: UniProt: O59010 #2: Chemical | ChemComp-ASP / #3: Chemical | ChemComp-NA / #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: 4.6 Å3/Da / Density % sol: 73.28 % |
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Crystal grow | Temperature: 277 K / Method: vapor diffusion, hanging drop / pH: 4.5 / Details: PEG400, SODIUM CHLORIDE, CITRATE/TRIS / PH range: 4.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: NSLS / Beamline: X29A / Wavelength: 0.97 Å |
Detector | Type: ADSC QUANTUM 315r / Detector: CCD / Date: Jun 13, 2013 |
Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.97 Å / Relative weight: 1 |
Reflection | Resolution: 3.5→15 Å / Num. obs: 55613 / % possible obs: 98.1 % / Redundancy: 4.5 % / Rmerge(I) obs: 0.084 / Net I/σ(I): 10.6 |
Reflection shell | Resolution: 3.5→3.63 Å / Redundancy: 4.2 % / Mean I/σ(I) obs: 0.4 / % possible all: 96.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 2NWX Resolution: 3.5→15 Å / Cor.coef. Fo:Fc: 0.948 / Cor.coef. Fo:Fc free: 0.922 / SU B: 102.928 / SU ML: 0.619 / Cross valid method: THROUGHOUT / ESU R Free: 0.606 / 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: 152.9 Å2
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Refinement step | Cycle: LAST / Resolution: 3.5→15 Å
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Refine LS restraints |
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