+
Open data
-
Basic information
Entry | Database: PDB / ID: 2f66 | ||||||
---|---|---|---|---|---|---|---|
Title | Structure of the ESCRT-I endosomal trafficking complex | ||||||
![]() |
| ||||||
![]() | TRANSPORT PROTEIN / Endosome / Trafficking complex / Vps23 / Vps28 / Vps37 / Vacuolar Protein Sorting / ESCRT protein complexes / Endosomal Sorting Complex Required for Transport / ESCRT-I / ubiquitin / Tsg101 | ||||||
Function / homology | ![]() negative regulation of protein polyubiquitination / ESCRT I complex / ATP export / Endosomal Sorting Complex Required For Transport (ESCRT) / endosome transport via multivesicular body sorting pathway / protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / protein targeting to vacuole / late endosome to vacuole transport / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / protein targeting to membrane ...negative regulation of protein polyubiquitination / ESCRT I complex / ATP export / Endosomal Sorting Complex Required For Transport (ESCRT) / endosome transport via multivesicular body sorting pathway / protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / protein targeting to vacuole / late endosome to vacuole transport / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / protein targeting to membrane / reticulophagy / endosome to lysosome transport / ubiquitin binding / protein modification process / cytoplasmic side of plasma membrane / late endosome membrane / endosome / protein-containing complex binding / nucleus / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Kostelansky, M.S. / Lee, S. / Kim, J. / Hurley, J.H. | ||||||
![]() | ![]() Title: Structural and functional organization of the ESCRT-I trafficking complex. Authors: Kostelansky, M.S. / Sun, J. / Lee, S. / Kim, J. / Ghirlando, R. / Hierro, A. / Emr, S.D. / Hurley, J.H. | ||||||
History |
|
-
Structure visualization
Structure viewer | Molecule: ![]() ![]() |
---|
-
Downloads & links
-
Download
PDBx/mmCIF format | ![]() | 109.7 KB | Display | ![]() |
---|---|---|---|---|
PDB format | ![]() | 85.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 486.8 KB | Display | ![]() |
---|---|---|---|---|
Full document | ![]() | 499.7 KB | Display | |
Data in XML | ![]() | 20.2 KB | Display | |
Data in CIF | ![]() | 26.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2f6mSC S: Starting model for refinement C: citing same article ( |
---|---|
Similar structure data |
-
Links
-
Assembly
Deposited unit | ![]()
| ||||||||
---|---|---|---|---|---|---|---|---|---|
1 | ![]()
| ||||||||
2 | ![]()
| ||||||||
3 |
| ||||||||
Unit cell |
|
-
Components
#1: Protein | Mass: 7550.657 Da / Num. of mol.: 2 / Fragment: Vps23C-Terminal Domain (322-385) / Mutation: C344A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: STP22, VPS23 / Plasmid: pST39 / Species (production host): Escherichia coli / Production host: ![]() ![]() #2: Protein | Mass: 13296.793 Da / Num. of mol.: 2 / Fragment: Vps28N-Terminal Domain (13-125) / Mutation: C101A Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: VPS28, VPT28 / Plasmid: pST39 / Species (production host): Escherichia coli / Production host: ![]() ![]() #3: Protein | Mass: 9833.885 Da / Num. of mol.: 2 / Fragment: Vps37C-Terminal Domain (132-213) Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Gene: SRN2, VPS37 / Plasmid: pST39 / Species (production host): Escherichia coli / Production host: ![]() ![]() #4: Chemical | #5: Water | ChemComp-HOH / | |
---|
-Experimental details
-Experiment
Experiment | Method: ![]() |
---|
-
Sample preparation
Crystal | Density Matthews: 3.02 Å3/Da / Density % sol: 59.26 % |
---|---|
Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 5.6 Details: 100mM trisodium citrate (pH 5.6), 900mM lithium sulfate, 500mM ammonium sulfate, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
-Data collection
Diffraction | Mean temperature: 100 K |
---|---|
Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: MARRESEARCH / Detector: CCD / Date: Jul 29, 2005 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9795 Å / Relative weight: 1 |
Reflection | Resolution: 2.8→20 Å / Num. all: 17885 / Num. obs: 17872 / % possible obs: 95.9 % / Redundancy: 4.1 % / Biso Wilson estimate: 62.9 Å2 / Rsym value: 0.088 / Net I/σ(I): 15.7 |
Reflection shell | Resolution: 2.8→2.9 Å / Redundancy: 2.8 % / Mean I/σ(I) obs: 2.1 / Num. unique all: 17885 / Rsym value: 0.449 / % possible all: 76.7 |
-
Processing
Software |
| |||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
Refinement | Method to determine structure: ![]() Starting model: Vps23C/Vps28N complex structure, PDB Code 2F6M Resolution: 2.8→19.93 Å / Rfactor Rfree error: 0.009 / Data cutoff high absF: 2114242.17 / Data cutoff low absF: 0 / Isotropic thermal model: RESTRAINED / Cross valid method: THROUGHOUT / Stereochemistry target values: Engh & Huber
| |||||||||||||||||||||||||
Solvent computation | Solvent model: FLAT MODEL / Bsol: 32.9325 Å2 / ksol: 0.35178 e/Å3 | |||||||||||||||||||||||||
Displacement parameters | Biso mean: 58 Å2
| |||||||||||||||||||||||||
Refine analyze |
| |||||||||||||||||||||||||
Refinement step | Cycle: LAST / Resolution: 2.8→19.93 Å
| |||||||||||||||||||||||||
Refine LS restraints |
| |||||||||||||||||||||||||
LS refinement shell | Resolution: 2.8→2.97 Å / Rfactor Rfree error: 0.03 / Total num. of bins used: 6
| |||||||||||||||||||||||||
Xplor file |
|