+Open data
-Basic information
Entry | Database: PDB / ID: 5hw6 | ||||||
---|---|---|---|---|---|---|---|
Title | Candida albicans FKBP12 apo protein in C2 space group | ||||||
Components | FK506-binding protein 1 | ||||||
Keywords | ISOMERASE / FKBP12 / prolyl isomerase | ||||||
Function / homology | Function and homology information regulation of homoserine biosynthetic process / fungal biofilm matrix / macrolide binding / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / protein folding / chromatin organization / extracellular region / cytoplasm Similarity search - Function | ||||||
Biological species | Candida albicans (yeast) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.401 Å | ||||||
Authors | Tonthat, N.K. / Schumacher, M.A. | ||||||
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 |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 5hw6.cif.gz | 136 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb5hw6.ent.gz | 109.1 KB | Display | PDB format |
PDBx/mmJSON format | 5hw6.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/hw/5hw6 ftp://data.pdbj.org/pub/pdb/validation_reports/hw/5hw6 | HTTPS FTP |
---|
-Related structure data
Related structure data | 5ht1C 5htgC 5huaC 5hw7C 5hw8C 5hwbC 5hwcC 5i98C 5j6eC C: citing same article (ref.) |
---|---|
Similar structure data |
-Links
-Assembly
Deposited unit |
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
2 |
| ||||||||
Unit cell |
|
-Components
#1: Protein | Mass: 13062.796 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Candida albicans (strain SC5314 / ATCC MYA-2876) (yeast) Strain: SC5314 / ATCC MYA-2876 Gene: RBP1, RBP11, CaO19.11186, CaO19.3702, RBP2, RBP12, CaJ7.0299, CaO19.13810, CaO19.6452 Production host: Escherichia coli (E. coli) / References: UniProt: P28870, peptidylprolyl isomerase #2: Chemical | ChemComp-ACT / | #3: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
---|
-Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46.64 % |
---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop Details: 25% PEG 8000, 0.1 M Sodium acetate pH 4.5 and 0.2M Lithium Sulfate |
-Data collection
Diffraction | Mean temperature: 100 K | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Diffraction source | Source: SYNCHROTRON / Site: APS / Beamline: 22-BM / Wavelength: 1 Å | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Detector | Type: MAR CCD 130 mm / Detector: CCD / Date: Mar 21, 2012 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Radiation wavelength | Wavelength: 1 Å / Relative weight: 1 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection | Resolution: 2.4→50 Å / Num. obs: 9189 / % possible obs: 98.2 % / Redundancy: 3.3 % / Rmerge(I) obs: 0.101 / Χ2: 1.373 / Net I/av σ(I): 13.152 / Net I/σ(I): 13.1 / Num. measured all: 30224 | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Reflection shell |
|
-Processing
Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: MOLECULAR REPLACEMENT / Resolution: 2.401→25.96 Å / SU ML: 0.14 / Cross valid method: FREE R-VALUE / σ(F): 0.21 / Phase error: 20.74
| |||||||||||||||||||||||||||||||||||||||||||||||||
Solvent computation | Shrinkage radii: 0.6 Å / VDW probe radii: 0.9 Å / Bsol: 39.451 Å2 / ksol: 0.402 e/Å3 | |||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 67.41 Å2 / Biso mean: 24.5815 Å2 / Biso min: 1.96 Å2
| |||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.401→25.96 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||
LS refinement shell | Refine-ID: X-RAY DIFFRACTION / Total num. of bins used: 6
| |||||||||||||||||||||||||||||||||||||||||||||||||
Refinement TLS params. | Method: refined / Origin x: 38.1895 Å / Origin y: -34.8848 Å / Origin z: 14.1222 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||
Refinement TLS group |
|