+
Open data
-
Basic information
Entry | Database: PDB / ID: 3frv | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of Human CHMP3 (residues 1-150) | ||||||
![]() | Charged multivesicular body protein 3 | ||||||
![]() | PROTEIN TRANSPORT / ESCRT / ESCRT-III / CHMP / IST1 / Coiled coil / Cytoplasm / Lipoprotein / Membrane / Myristate / Phosphoprotein / Transport | ||||||
Function / homology | ![]() regulation of endosome size / amphisome membrane / multivesicular body-lysosome fusion / vesicle fusion with vacuole / suppression of viral release by host / late endosome to lysosome transport / ESCRT III complex / kinetochore microtubule / endosome transport via multivesicular body sorting pathway / regulation of centrosome duplication ...regulation of endosome size / amphisome membrane / multivesicular body-lysosome fusion / vesicle fusion with vacuole / suppression of viral release by host / late endosome to lysosome transport / ESCRT III complex / kinetochore microtubule / endosome transport via multivesicular body sorting pathway / regulation of centrosome duplication / nuclear membrane reassembly / Sealing of the nuclear envelope (NE) by ESCRT-III / midbody abscission / multivesicular body sorting pathway / membrane fission / plasma membrane repair / late endosome to vacuole transport / phosphatidylcholine binding / multivesicular body membrane / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / multivesicular body assembly / regulation of mitotic spindle assembly / Translation of Replicase and Assembly of the Replication Transcription Complex / regulation of early endosome to late endosome transport / mitotic metaphase chromosome alignment / Macroautophagy / molecular function inhibitor activity / nucleus organization / ubiquitin-specific protease binding / viral budding via host ESCRT complex / positive regulation of cytokinesis / autophagosome membrane / autophagosome maturation / viral release from host cell / protein polymerization / Pyroptosis / nuclear pore / Endosomal Sorting Complex Required For Transport (ESCRT) / phosphatidylinositol-4,5-bisphosphate binding / multivesicular body / viral budding from plasma membrane / HCMV Late Events / macroautophagy / Late endosomal microautophagy / Budding and maturation of HIV virion / kinetochore / autophagy / protein transport / late endosome / Translation of Replicase and Assembly of the Replication Transcription Complex / midbody / cytoplasmic vesicle / early endosome / lysosomal membrane / apoptotic process / extracellular exosome / identical protein binding / plasma membrane / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Hill, C.P. / Schubert, H.L. / McCullough, J. / Sundquist, W.I. | ||||||
![]() | ![]() Title: Structural basis for ESCRT-III protein autoinhibition. Authors: Bajorek, M. / Schubert, H.L. / McCullough, J. / Langelier, C. / Eckert, D.M. / Stubblefield, W.M. / Uter, N.T. / Myszka, D.G. / Hill, C.P. / Sundquist, W.I. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 37.7 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 25.9 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 425.7 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 431.3 KB | Display | |
Data in XML | ![]() | 7.9 KB | Display | |
Data in CIF | ![]() | 9.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 3frrC ![]() 3frsC ![]() 3frtC ![]() 2gd5S C: citing same article ( S: Starting model for refinement |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 17408.699 Da / Num. of mol.: 1 / Fragment: UNP residues 1 - 150 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() ![]() |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.15 Å3/Da / Density % sol: 60.95 % |
---|---|
Crystal grow | Temperature: 286 K / Method: vapor diffusion, sitting drop / pH: 7.5 Details: 16% PEG 3350, 100 mM HEPES, 200mM Proline, pH 7.5, VAPOR DIFFUSION, SITTING DROP, temperature 286K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() |
Detector | Type: RIGAKU RAXIS IV / Detector: IMAGE PLATE / Date: Nov 25, 2008 / Details: Verimax HR |
Radiation | Monochromator: verimax HR / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 1.54 Å / Relative weight: 1 |
Reflection | Resolution: 3.7→25 Å / Num. all: 2586 / Num. obs: 2451 / % possible obs: 99.2 % / Observed criterion σ(F): 0 / Observed criterion σ(I): 0 / Redundancy: 3.2 % / Biso Wilson estimate: 101 Å2 / Rmerge(I) obs: 0.63 / Net I/σ(I): 18.3 |
Reflection shell | Resolution: 3.7→3.83 Å / Redundancy: 3.1 % / Rmerge(I) obs: 0.553 / Mean I/σ(I) obs: 2.2 / % possible all: 99.2 |
-
Processing
Software |
| ||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: PDB ENTRY 2GD5 Resolution: 3.7→25 Å / σ(F): 0 / Stereochemistry target values: Engh & Huber Details: rigid body only - against anisotropically adjusted Fs by PHASER.
| ||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 3.7→25 Å
|