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Open data
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Basic information
Entry | Database: PDB / ID: 1n1a | ||||||
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Title | Crystal Structure of the N-terminal domain of human FKBP52 | ||||||
![]() | FKBP52 | ||||||
![]() | ISOMERASE / FKBP52 / the N-terminal domain | ||||||
Function / homology | ![]() steroid hormone receptor complex assembly / negative regulation of microtubule polymerization or depolymerization / male sex differentiation / copper-dependent protein binding / prostate gland development / copper ion transport / nuclear glucocorticoid receptor binding / protein-containing complex localization / negative regulation of microtubule polymerization / FK506 binding ...steroid hormone receptor complex assembly / negative regulation of microtubule polymerization or depolymerization / male sex differentiation / copper-dependent protein binding / prostate gland development / copper ion transport / nuclear glucocorticoid receptor binding / protein-containing complex localization / negative regulation of microtubule polymerization / FK506 binding / androgen receptor signaling pathway / Attenuation phase / axonal growth cone / chaperone-mediated protein folding / heat shock protein binding / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / embryo implantation / ESR-mediated signaling / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / phosphoprotein binding / tau protein binding / negative regulation of neuron projection development / protein folding / protein-macromolecule adaptor activity / Estrogen-dependent gene expression / microtubule / Potential therapeutics for SARS / neuronal cell body / GTP binding / perinuclear region of cytoplasm / protein-containing complex / mitochondrion / RNA binding / extracellular exosome / nucleoplasm / ATP binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Li, P. / Ding, Y. / Wu, B. / Shu, C. / Shen, B. / Rao, Z. | ||||||
![]() | ![]() Title: Structure of the N-terminal domain of human FKBP52. Authors: Li, P. / Ding, Y. / Wu, B. / Shu, C. / Shen, B. / Rao, Z. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 58.7 KB | Display | ![]() |
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PDB format | ![]() | 43 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 1fkjS S: Starting model for refinement |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Details | The biological assembly is a dimer in the asymmetric unit |
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Components
#1: Protein | Mass: 15336.519 Da / Num. of mol.: 2 / Fragment: the N-terminal fragment (1-140) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 1.85 Å3/Da / Density % sol: 33.68 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 291 K / Method: vapor diffusion, hanging drop / pH: 8.5 Details: Tris-HCl, Ammonium Sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() |
Detector | Type: MARRESEARCH / Detector: IMAGE PLATE / Date: Jan 1, 2001 / Details: mirrors |
Radiation | Monochromator: CuKa / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.4→40 Å / Num. all: 26262 / Num. obs: 26259 / % possible obs: 99.9 % / Observed criterion σ(F): 1 / Observed criterion σ(I): 1 / Redundancy: 10.8 % / Rmerge(I) obs: 0.095 / Net I/σ(I): 17.3 |
Reflection shell | Resolution: 2.4→2.49 Å / Redundancy: 8.4 % / Rmerge(I) obs: 0.294 / Mean I/σ(I) obs: 9.3 / Num. unique all: 8929 / % possible all: 99.9 |
Reflection | *PLUS Lowest resolution: 40 Å / Num. obs: 8929 / Num. measured all: 26262 |
Reflection shell | *PLUS Highest resolution: 2.4 Å / % possible obs: 99.9 % / Num. unique obs: 889 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1FKJ Resolution: 2.4→40 Å / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Displacement parameters |
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Refinement step | Cycle: LAST / Resolution: 2.4→40 Å
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Refine LS restraints |
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Xplor file |
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Refinement | *PLUS Lowest resolution: 40 Å | |||||||||||||||||||||||||
Solvent computation | *PLUS | |||||||||||||||||||||||||
Displacement parameters | *PLUS | |||||||||||||||||||||||||
Refine LS restraints | *PLUS
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