[English] 日本語
![](img/lk-miru.gif)
- PDB-2fap: THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-(C16)-... -
+
Open data
-
Basic information
Entry | Database: PDB / ID: 2fap | ||||||
---|---|---|---|---|---|---|---|
Title | THE STRUCTURE OF THE IMMUNOPHILIN-IMMUNOSUPPRESSANT FKBP12-(C16)-ETHOXY RAPAMYCIN COMPLEX INTERACTING WITH HUMA | ||||||
![]() |
| ||||||
![]() | COMPLEX (ISOMERASE/KINASE) / FKBP12 / FRAP / RAPAMYCIN / COMPLEX (ISOMERASE-KINASE) / COMPLEX (ISOMERASE-KINASE) complex | ||||||
Function / homology | ![]() positive regulation of cytoplasmic translational initiation / positive regulation of pentose-phosphate shunt / RNA polymerase III type 1 promoter sequence-specific DNA binding / RNA polymerase III type 2 promoter sequence-specific DNA binding / T-helper 1 cell lineage commitment / regulation of locomotor rhythm / positive regulation of wound healing, spreading of epidermal cells / cellular response to leucine starvation / regulation of membrane permeability / heart valve morphogenesis ...positive regulation of cytoplasmic translational initiation / positive regulation of pentose-phosphate shunt / RNA polymerase III type 1 promoter sequence-specific DNA binding / RNA polymerase III type 2 promoter sequence-specific DNA binding / T-helper 1 cell lineage commitment / regulation of locomotor rhythm / positive regulation of wound healing, spreading of epidermal cells / cellular response to leucine starvation / regulation of membrane permeability / heart valve morphogenesis / TFIIIC-class transcription factor complex binding / negative regulation of lysosome organization / macrolide binding / RNA polymerase III type 3 promoter sequence-specific DNA binding / TORC2 complex / activin receptor binding / TORC1 complex / positive regulation of transcription of nucleolar large rRNA by RNA polymerase I / cytoplasmic side of membrane / regulation of autophagosome assembly / calcineurin-NFAT signaling cascade / nucleus localization / TORC1 signaling / voluntary musculoskeletal movement / regulation of osteoclast differentiation / positive regulation of keratinocyte migration / signaling receptor inhibitor activity / transforming growth factor beta receptor binding / TGFBR1 LBD Mutants in Cancer / cellular response to L-leucine / MTOR signalling / Amino acids regulate mTORC1 / cellular response to nutrient / energy reserve metabolic process / type I transforming growth factor beta receptor binding / Energy dependent regulation of mTOR by LKB1-AMPK / negative regulation of activin receptor signaling pathway / negative regulation of cell size / heart trabecula formation / ruffle organization / cellular response to osmotic stress / terminal cisterna / ryanodine receptor complex / I-SMAD binding / negative regulation of protein localization to nucleus / anoikis / regulation of amyloid precursor protein catabolic process / cardiac muscle cell development / positive regulation of transcription by RNA polymerase III / protein maturation by protein folding / negative regulation of calcineurin-NFAT signaling cascade / ventricular cardiac muscle tissue morphogenesis / 'de novo' protein folding / regulation of myelination / regulation of cell size / Macroautophagy / negative regulation of phosphoprotein phosphatase activity / positive regulation of oligodendrocyte differentiation / negative regulation of macroautophagy / FK506 binding / positive regulation of actin filament polymerization / lysosome organization / positive regulation of myotube differentiation / behavioral response to pain / oligodendrocyte differentiation / mTORC1-mediated signalling / TGF-beta receptor signaling activates SMADs / Constitutive Signaling by AKT1 E17K in Cancer / germ cell development / CD28 dependent PI3K/Akt signaling / cellular response to nutrient levels / positive regulation of phosphoprotein phosphatase activity / Calcineurin activates NFAT / HSF1-dependent transactivation / regulation of immune response / TOR signaling / neuronal action potential / positive regulation of translational initiation / response to amino acid / regulation of macroautophagy / endomembrane system / 'de novo' pyrimidine nucleobase biosynthetic process / protein peptidyl-prolyl isomerization / positive regulation of epithelial to mesenchymal transition / positive regulation of lamellipodium assembly / positive regulation of lipid biosynthetic process / supramolecular fiber organization / heart morphogenesis / cardiac muscle contraction / regulation of cellular response to heat / regulation of ryanodine-sensitive calcium-release channel activity / positive regulation of stress fiber assembly / cytoskeleton organization / sarcoplasmic reticulum membrane / T cell costimulation / T cell activation / cellular response to amino acid starvation / positive regulation of glycolytic process / cellular response to starvation / phagocytic vesicle Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Liang, J. / Choi, J. / Clardy, J. | ||||||
![]() | ![]() Title: Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2 A resolution. Authors: Liang, J. / Choi, J. / Clardy, J. #1: ![]() Title: Structure of the Fkbp12-Rapamycin Complex Interacting with the Binding Domain of Human Frap Authors: Choi, J. / Chen, J. / Schreiber, S.L. / Clardy, J. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 60.3 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 41.7 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 858.6 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 862 KB | Display | |
Data in XML | ![]() | 7.4 KB | Display | |
Data in CIF | ![]() | 10.1 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 1nsgC ![]() 3fapC ![]() 4fapC ![]() 1fapS S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 11836.508 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: HUMAN HIPPOCAMPAL CDNA LIBRARY (CLONTECH, PALO ALTO, CA) Plasmid: PGEX-3X / Production host: ![]() ![]() |
---|---|
#2: Protein | Mass: 11331.937 Da / Num. of mol.: 1 / Fragment: FRB Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
#3: Chemical | ChemComp-RAD / |
#4: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 2.58 Å3/Da / Density % sol: 52 % | ||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Crystal grow | pH: 8.5 / Details: pH 8.5 | ||||||||||||||||||||||||||||||||||||
Crystal | *PLUS Density % sol: 51 % | ||||||||||||||||||||||||||||||||||||
Crystal grow | *PLUS pH: 8 / Method: vapor diffusion, hanging drop / Details: used to seeding | ||||||||||||||||||||||||||||||||||||
Components of the solutions | *PLUS
|
-Data collection
Diffraction | Mean temperature: 298 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: XUONG-HAMLIN MULTIWIRE / Detector: AREA DETECTOR / Date: Jul 29, 1996 |
Radiation | Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.5418 Å / Relative weight: 1 |
Reflection | Resolution: 2.2→100 Å / Num. obs: 12865 / % possible obs: 97.4 % / Observed criterion σ(I): 0 / Redundancy: 3 % / Rmerge(I) obs: 0.087 |
Reflection shell | Resolution: 2.2→2.3 Å / Rmerge(I) obs: 0.27 / % possible all: 90.8 |
Reflection | *PLUS Num. measured all: 30805 |
Reflection shell | *PLUS % possible obs: 90.8 % |
-
Processing
Software |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 1FAP Resolution: 2.2→8 Å / Isotropic thermal model: RESTRAINED / Cross valid method: RFREE / σ(F): 0
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 15.6 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.2→8 Å
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Xplor file |
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Software | *PLUS Name: ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refine LS restraints | *PLUS
|