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Open data
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Basic information
Entry | Database: PDB / ID: 1u5t | ||||||
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Title | Structure of the ESCRT-II endosomal trafficking complex | ||||||
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![]() | TRANSPORT PROTEIN / escrt / endosomal / trafficking / protein complex | ||||||
Function / homology | ![]() ESCRT II complex / carbon catabolite repression of transcription from RNA polymerase II promoter by glucose / ATP export / protein retention in Golgi apparatus / Endosomal Sorting Complex Required For Transport (ESCRT) / cytoplasm to vacuole targeting by the Cvt pathway / protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / protein targeting to vacuole / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / phosphatidylinositol-3-phosphate binding ...ESCRT II complex / carbon catabolite repression of transcription from RNA polymerase II promoter by glucose / ATP export / protein retention in Golgi apparatus / Endosomal Sorting Complex Required For Transport (ESCRT) / cytoplasm to vacuole targeting by the Cvt pathway / protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / protein targeting to vacuole / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / phosphatidylinositol-3-phosphate binding / localization / ubiquitin binding / macroautophagy / late endosome membrane / lipid binding / structural molecule activity / protein homodimerization activity / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ![]() ![]() | ||||||
![]() | Hierro, A. / Sun, J. / Rusnak, A.S. / Kim, J. / Prag, G. / Emr, S.D. / Hurley, J.H. | ||||||
![]() | ![]() Title: Structure of ESCRT-II endosomal trafficking complex Authors: Hierro, A. / Sun, J. / Rusnak, A.S. / Kim, J. / Prag, G. / Emr, S.D. / Hurley, J.H. #1: ![]() Title: ESCRT-II, an endosome-associated complex required for protein sorting: Crystal structure and interactions with ESCRT-III and membranes Authors: Teo, H. / Perisic, O. / Gonzalez, B. / Williams, R.L. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 161.7 KB | Display | ![]() |
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PDB format | ![]() | 128.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 450.5 KB | Display | ![]() |
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Full document | ![]() | 580.1 KB | Display | |
Data in XML | ![]() | 44.7 KB | Display | |
Data in CIF | ![]() | 59.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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Unit cell |
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Components
#1: Protein | Mass: 26988.092 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: pST39 / Species (production host): Escherichia coli / Production host: ![]() ![]() |
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#2: Protein | Mass: 19657.611 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: pST39 / Species (production host): Escherichia coli / Production host: ![]() ![]() |
#3: Protein | Mass: 23582.650 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Plasmid: pST39 / Species (production host): Escherichia coli / Production host: ![]() ![]() |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 5.57 Å3/Da / Density % sol: 77.93 % |
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Crystal grow | Temperature: 298 K / Method: vapor diffusion, hanging drop / pH: 7.4 Details: Naacetate, hepes, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K |
-Data collection
Detector | Date: Feb 12, 2004 |
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Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Relative weight: 1 |
Reflection | Resolution: 3.6→6 Å / Num. all: 44800 / Num. obs: 41210 / % possible obs: 91.9 % |
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Processing
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Refinement | Method to determine structure: ![]()
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Refinement step | Cycle: LAST / Resolution: 3.6→6 Å
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Refine LS restraints |
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