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Open data
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Basic information
Entry | Database: PDB / ID: 1ejf | ||||||
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Title | CRYSTAL STRUCTURE OF THE HUMAN CO-CHAPERONE P23 | ||||||
![]() | Prostaglandin E synthase 3 | ||||||
![]() | CHAPERONE / Co-Chaperone / Beta-Sandwich | ||||||
Function / homology | ![]() lung saccule development / prostaglandin-E synthase / prostaglandin-E synthase activity / telomerase activity / nuclear receptor-mediated glucocorticoid signaling pathway / Aryl hydrocarbon receptor signalling / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / cyclooxygenase pathway / telomerase holoenzyme complex / glycogen biosynthetic process ...lung saccule development / prostaglandin-E synthase / prostaglandin-E synthase activity / telomerase activity / nuclear receptor-mediated glucocorticoid signaling pathway / Aryl hydrocarbon receptor signalling / Synthesis of Prostaglandins (PG) and Thromboxanes (TX) / cyclooxygenase pathway / telomerase holoenzyme complex / glycogen biosynthetic process / protein folding chaperone complex / prostaglandin biosynthetic process / skin development / telomerase holoenzyme complex assembly / : / chaperone cofactor-dependent protein refolding / telomere maintenance via telomerase / chaperone-mediated protein complex assembly / HSF1 activation / Attenuation phase / DNA polymerase binding / positive regulation of phosphorylation / HSP90 chaperone cycle for steroid hormone receptors (SHR) in the presence of ligand / telomere maintenance / ESR-mediated signaling / Hsp90 protein binding / unfolded protein binding / protein folding / protein-folding chaperone binding / fibroblast proliferation / Estrogen-dependent gene expression / Potential therapeutics for SARS / chromosome, telomeric region / protein stabilization / signal transduction / protein-containing complex / nucleoplasm / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Weaver, A.J. / Sullivan, W.P. / Felts, S.J. / Owen, B.A.L. / Toft, D.O. | ||||||
![]() | ![]() Title: Crystal structure and activity of human p23, a heat shock protein 90 co-chaperone. Authors: Weaver, A.J. / Sullivan, W.P. / Felts, S.J. / Owen, B.A. / Toft, D.O. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 54.6 KB | Display | ![]() |
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PDB format | ![]() | 43.5 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Similar structure data |
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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: 14892.471 Da / Num. of mol.: 2 / Fragment: RESIDUES 1-125 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() #2: Chemical | #3: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.61 Å3/Da / Density % sol: 52.88 % | ||||||||||||||||||||||||||||||
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 9 Details: ammonium sulfate, bicine, tris, pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 298K | ||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 7.5 | ||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
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-Data collection
Diffraction | Mean temperature: 93 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: ADSC QUANTUM 4 / Detector: CCD / Date: Dec 31, 1998 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9159 Å / Relative weight: 1 |
Reflection | Resolution: 2.49→100 Å / Num. all: 11727 / Num. obs: 11651 / % possible obs: 99.4 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 8.3 % / Biso Wilson estimate: 37.6 Å2 / Rmerge(I) obs: 0.05 / Net I/σ(I): 7.7 |
Reflection shell | Resolution: 2.49→2.62 Å / Redundancy: 6.8 % / Rmerge(I) obs: 0.074 / % possible all: 98.8 |
Reflection | *PLUS Lowest resolution: 15 Å / Num. obs: 11743 / Num. measured all: 97860 / Rmerge(I) obs: 0.05 |
Reflection shell | *PLUS % possible obs: 98.8 % / Num. unique obs: 1651 / Num. measured obs: 11297 / Mean I/σ(I) obs: 8.7 |
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Processing
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Refinement | Resolution: 2.49→100 Å / Rfactor Rfree error: 0.011 / Data cutoff high absF: 1000000 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / σ(F): 0 / σ(I): 0 / Stereochemistry target values: Engh & Huber
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Solvent computation | Solvent model: FLAT MODEL / Bsol: 27.8 Å2 / ksol: 0.374 e/Å3 | ||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31.2 Å2
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Refine analyze |
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Refinement step | Cycle: LAST / Resolution: 2.49→100 Å
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Refine LS restraints |
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LS refinement shell | Resolution: 2.49→2.65 Å / Rfactor Rfree error: 0.042 / Total num. of bins used: 6
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Xplor file |
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Refinement | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 15 Å / σ(F): 0 / % reflection Rfree: 4.8 % / Rfactor obs: 0.236 | ||||||||||||||||||||||||||||||||||||
Solvent computation | *PLUS | ||||||||||||||||||||||||||||||||||||
Displacement parameters | *PLUS Biso mean: 31.2 Å2 | ||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
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LS refinement shell | *PLUS % reflection Rfree: 5 % / Rfactor Rwork: 0.3 |