+Open data
-Basic information
Entry | Database: PDB / ID: 5j6e | ||||||
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Title | Structure of disulfide crosslinked A. fumigatus FKBP12(V91C) | ||||||
Components | FK506-binding protein 1A | ||||||
Keywords | ISOMERASE / FKBP12 / disulfide trapping / crosslinked dimer | ||||||
Function / homology | Function and homology information peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Neosartorya fumigata (mold) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / molecular replacement / Resolution: 3.2 Å | ||||||
Authors | Schumacher, M. | ||||||
Citation | Journal: Mbio / Year: 2016 Title: Structures of Pathogenic Fungal FKBP12s Reveal Possible Self-Catalysis Function. Authors: Tonthat, N.K. / Juvvadi, P.R. / Zhang, H. / Lee, S.C. / Venters, R. / Spicer, L. / Steinbach, W.J. / Heitman, J. / Schumacher, M.A. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5j6e.cif.gz | 50.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5j6e.ent.gz | 39.6 KB | Display | PDB format |
PDBx/mmJSON format | 5j6e.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5j6e_validation.pdf.gz | 428.8 KB | Display | wwPDB validaton report |
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Full document | 5j6e_full_validation.pdf.gz | 432.3 KB | Display | |
Data in XML | 5j6e_validation.xml.gz | 10 KB | Display | |
Data in CIF | 5j6e_validation.cif.gz | 12.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j6/5j6e ftp://data.pdbj.org/pub/pdb/validation_reports/j6/5j6e | HTTPS FTP |
-Related structure data
Related structure data | 5ht1C 5htgC 5huaC 5hw6C 5hw7C 5hw8C 5hwbC 5hwcC 5i98C C: citing same article (ref.) |
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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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-Components
#1: Protein | Mass: 12076.637 Da / Num. of mol.: 2 / Mutation: V91C Source method: isolated from a genetically manipulated source Source: (gene. exp.) Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (mold) Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100 / Gene: fpr1A, AFUA_6G12170 / Production host: Escherichia coli (E. coli) / References: UniProt: Q4WLV6, peptidylprolyl isomerase |
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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: 3.7 Å3/Da / Density % sol: 66.75 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop Details: 1.5 M sodium citrate, sodium cacodylate buffer pH 6.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ALS / Beamline: 8.3.1 / Wavelength: 1 Å |
Detector | Type: ADSC QUANTUM 210r / Detector: CCD / Date: Feb 23, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 |
Reflection | Resolution: 3.02→44.807 Å / Num. obs: 10597 / % possible obs: 92.77 % / Redundancy: 2 % / Net I/σ(I): 8.9 |
Reflection shell | Highest resolution: 3.02 Å |
-Phasing
Phasing | Method: molecular replacement |
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-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 3.2→44.807 Å / SU ML: 0.38 / Cross valid method: FREE R-VALUE / σ(F): 1.28 / Phase error: 26.6
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Solvent computation | Shrinkage radii: 0.95 Å / VDW probe radii: 1.2 Å / Bsol: 0.001 Å2 / ksol: 0.329 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 135.89 Å2 / Biso mean: 19.35 Å2 / Biso min: 5.01 Å2
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Refinement step | Cycle: final / Resolution: 3.2→44.807 Å
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Refine LS restraints |
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LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 8
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