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Open data
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Basic information
Entry | Database: PDB / ID: 8z38 | ||||||
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Title | FK506 binding protein 1B (including FK506) | ||||||
![]() | peptidylprolyl isomerase | ||||||
![]() | PROTEIN BINDING / FK506 / FK506 binding protein 1B | ||||||
Function / homology | FKBP-type peptidyl-prolyl cis-trans isomerase domain profile. / FKBP-type peptidyl-prolyl cis-trans isomerase domain / FKBP-type peptidyl-prolyl cis-trans isomerase / Peptidyl-prolyl cis-trans isomerase domain superfamily / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / cytoplasm / 6-CARBOXYPIPERIDINE / peptidylprolyl isomerase![]() | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Liu, X.H. / Zhao, W.H. | ||||||
Funding support | ![]()
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![]() | ![]() Title: High-resolution cocrystallized crystal structures of FK506 and FK506-binding proteins Authors: Liu, X.H. / Zhao, W.H. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 66.8 KB | Display | ![]() |
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PDB format | ![]() | 39.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 714.7 KB | Display | ![]() |
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Full document | ![]() | 715.5 KB | Display | |
Data in XML | ![]() | 10.9 KB | Display | |
Data in CIF | ![]() | 14.4 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Unit cell |
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Components
#1: Protein | Mass: 11987.425 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | ChemComp-CPI / | #3: Water | ChemComp-HOH / | Has ligand of interest | Y | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 46.45 % |
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Crystal grow | Temperature: 291.15 K / Method: vapor diffusion, hanging drop Details: 0.1 M HEPES pH 7.5, 1.4 M tri-Sodium Citrate dihydrate or 2.1 M DL-Malic Acid pH 7.0. |
-Data collection
Diffraction | Mean temperature: 100 K / Serial crystal experiment: N |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS EIGER2 S 9M / Detector: PIXEL / Date: Sep 6, 2023 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.987 Å / Relative weight: 1 |
Reflection | Resolution: 2.17→42.65 Å / Num. obs: 10844 / % possible obs: 88.93 % / Redundancy: 5.6 % / Biso Wilson estimate: 26.41 Å2 / CC1/2: 0.99 / Rmerge(I) obs: 0.1712 / Rpim(I) all: 0.07119 / Rrim(I) all: 0.1866 / Net I/σ(I): 6.74 |
Reflection shell | Resolution: 2.17→2.248 Å / Rmerge(I) obs: 0.7258 / Mean I/σ(I) obs: 2.4 / Num. unique obs: 1114 / CC1/2: 0.758 / Rpim(I) all: 0.3117 / Rrim(I) all: 0.7951 |
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Processing
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Refinement | Method to determine structure: ![]() Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.1 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31.64 Å2 | |||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.17→42.65 Å
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Refine LS restraints |
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LS refinement shell |
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