[English] 日本語
![](img/lk-miru.gif)
- PDB-1yat: IMPROVED CALCINEURIN INHIBITION BY YEAST FKBP12-DRUG COMPLEXES. C... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 1yat | ||||||
---|---|---|---|---|---|---|---|
Title | IMPROVED CALCINEURIN INHIBITION BY YEAST FKBP12-DRUG COMPLEXES. CRYSTALLOGRAPHIC AND FUNCTIONAL ANALYSIS | ||||||
![]() | FK506 BINDING PROTEIN | ||||||
![]() | BINDING PROTEIN | ||||||
Function / homology | ![]() Calcineurin activates NFAT / regulation of homoserine biosynthetic process / macrolide binding / mTORC1-mediated signalling / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / protein folding / chromatin organization / mitochondrion / nucleus / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() | ||||||
![]() | Rotonda, J. / Becker, J.W. | ||||||
![]() | ![]() Title: Improved calcineurin inhibition by yeast FKBP12-drug complexes. Crystallographic and functional analysis. Authors: Rotonda, J. / Burbaum, J.J. / Chan, H.K. / Marcy, A.I. / Becker, J.W. #1: ![]() Title: Fk-506-Binding Protein: Three-Dimensional Structure of the Complex with the Antagonist L-685,818 Authors: Becker, J.W. / Rotonda, J. / Mckeever, B.M. / Chan, H.K. / Marcy, A.I. / Wiederrecht, G. / Hermes, J.D. / Springer, J.P. | ||||||
History |
| ||||||
Remark 700 | SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE ...SHEET THE SHEET STRUCTURE OF THIS MOLECULE IS BIFURCATED. IN ORDER TO REPRESENT THIS FEATURE IN THE SHEET RECORDS BELOW, TWO SIX-STRANDED SHEETS ARE DEFINED. STRANDS 1, 2, 3, 4, AND 5 ARE IDENTICAL IN BOTH SHEETS WHILE STRAND 6 IS DIFFERENT. |
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 35.4 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 23.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 838.1 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 843.8 KB | Display | |
Data in XML | ![]() | 8.5 KB | Display | |
Data in CIF | ![]() | 10.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
---|
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 12038.628 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() References: UniProt: P20081 |
---|---|
#2: Chemical | ChemComp-FK5 / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 4.11 Å3/Da / Density % sol: 70.09 % | ||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | *PLUS pH: 8.75 / Method: vapor diffusion | ||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Reflection | *PLUS Highest resolution: 2.5 Å / Num. obs: 6822 / % possible obs: 98 % / Num. measured all: 57469 / Rmerge(I) obs: 0.0977 |
---|
-
Processing
Software |
| ||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Resolution: 2.5→8 Å / σ(F): 0 /
| ||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.5→8 Å
| ||||||||||||
Refinement | *PLUS Highest resolution: 2.5 Å / Lowest resolution: 8 Å / Num. reflection all: 6822 / σ(F): 0 / Rfactor all: 0.177 | ||||||||||||
Solvent computation | *PLUS | ||||||||||||
Displacement parameters | *PLUS | ||||||||||||
Refine LS restraints | *PLUS
|