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Open data
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Basic information
| Entry | Database: PDB / ID: 1q0w | ||||||
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| Title | Solution structure of Vps27 amino-terminal UIM-ubiquitin complex | ||||||
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Keywords | TRANSPORT PROTEIN / PROTEIN-PROTEIN COMPLEX | ||||||
| Function / homology | Function and homology informationpositive regulation of protein maturation / microlipophagy / : / : / : / : / : / Regulation of TP53 Degradation / ESCRT-0 complex / : ...positive regulation of protein maturation / microlipophagy / : / : / : / : / : / Regulation of TP53 Degradation / ESCRT-0 complex / : / RAS processing / Regulation of PTEN localization / : / UCH proteinases / : / Aggrephagy / Pexophagy / PINK1-PRKN Mediated Mitophagy / : / Peroxisomal protein import / : / microautophagy / protein retention in Golgi apparatus / ABC-family proteins mediated transport / : / Endosomal Sorting Complex Required For Transport (ESCRT) / : / protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / ATP export / multivesicular body sorting pathway / Translesion synthesis by REV1 / : / : / protein targeting to vacuole / : / late endosome to vacuole transport / : / phosphatidylinositol-3-phosphate binding / ubiquitin-dependent protein catabolic process via the multivesicular body sorting pathway / Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks / : / cellular response to nitrogen starvation / vacuolar membrane / K48-linked polyubiquitin modification-dependent protein binding / K63-linked polyubiquitin modification-dependent protein binding / Formation of the ternary complex, and subsequently, the 43S complex / Ubiquitin-Mediated Degradation of Phosphorylated Cdc25A / Regulation of PTEN stability and activity / Ribosomal scanning and start codon recognition / CDK-mediated phosphorylation and removal of Cdc6 / FBXL7 down-regulates AURKA during mitotic entry and in early mitosis / KEAP1-NFE2L2 pathway / Neddylation / Formation of TC-NER Pre-Incision Complex / Orc1 removal from chromatin / Major pathway of rRNA processing in the nucleolus and cytosol / MAPK6/MAPK4 signaling / SRP-dependent cotranslational protein targeting to membrane / Gap-filling DNA repair synthesis and ligation in TC-NER / GTP hydrolysis and joining of the 60S ribosomal subunit / Formation of a pool of free 40S subunits / Nonsense Mediated Decay (NMD) independent of the Exon Junction Complex (EJC) / Nonsense Mediated Decay (NMD) enhanced by the Exon Junction Complex (EJC) / Antigen processing: Ubiquitination & Proteasome degradation / L13a-mediated translational silencing of Ceruloplasmin expression / Dual incision in TC-NER / protein secretion / ribosomal large subunit export from nucleus / Ub-specific processing proteases / ubiquitin binding / modification-dependent protein catabolic process / protein tag activity / peroxisome / ribosome biogenesis / ribosomal large subunit assembly / cytosolic large ribosomal subunit / cytoplasmic translation / endosome / endosome membrane / structural constituent of ribosome / protein ubiquitination / protein heterodimerization activity / protein domain specific binding / ubiquitin protein ligase binding / protein-containing complex / zinc ion binding / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
| Biological species | ![]() | ||||||
| Method | SOLUTION NMR / TORSION ANGLE DYNAMICS, SIMULATED ANNEALING | ||||||
Authors | Swanson, K.A. / Kang, R.S. / Stamenova, S.D. / Hicke, L. / Radhakrishnan, I. | ||||||
Citation | Journal: Embo J. / Year: 2003Title: Solution Structure of Vps27 UIM-Ubiquitin Complex Important for Endosomal Sorting and Receptor Downregulation Authors: Swanson, K.A. / Kang, R.S. / Stamenova, S.D. / Hicke, L. / Radhakrishnan, I. | ||||||
| History |
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| Remark 650 | HELIX Author determined secondary structure | ||||||
| Remark 700 | SHEET Author determined secondary structure |
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Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 1q0w.cif.gz | 627.1 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb1q0w.ent.gz | 524.4 KB | Display | PDB format |
| PDBx/mmJSON format | 1q0w.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/q0/1q0w ftp://data.pdbj.org/pub/pdb/validation_reports/q0/1q0w | HTTPS FTP |
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-Related structure data
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Links
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Assembly
| Deposited unit | ![]()
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| NMR ensembles |
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Components
| #1: Protein/peptide | Mass: 2824.103 Da / Num. of mol.: 1 / Fragment: Amino-terminal UIM, residues 256 to 278 / Source method: obtained synthetically Details: The sequence was synthesized using a peptide synthesizer. The sequence contains a non-native tyrosine residue at the amino-terminus (residue number 255). The sequence occurs naturally in S. Cerevisiae. References: UniProt: P40343 |
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| #2: Protein | Mass: 8568.769 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: (UBI1 OR RPL40A OR YIL148W) AND (UBI2 OR RPL40B OR YKR094C) AND (UBI3 OR RPS31 OR YLR167W OR L9470.14) AND (UBI4 OR SCD2 OR YLL039C) Plasmid: pET3-a / Species (production host): Escherichia coli / Production host: ![]() |
-Experimental details
-Experiment
| Experiment | Method: SOLUTION NMR | ||||||||||||||||||||||||
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| NMR experiment |
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Sample preparation
| Details |
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| Sample conditions | Ionic strength: 20 mM sodium phosphate, pH 6.0, 0.2% NaN3 / pH: 6 / Pressure: 1 atm / Temperature: 298 K | |||||||||
| Crystal grow | *PLUS Method: other / Details: NMR |
-NMR measurement
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M |
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| Radiation wavelength | Relative weight: 1 |
| NMR spectrometer | Type: Varian INOVA / Manufacturer: Varian / Model: INOVA / Field strength: 600 MHz |
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Processing
| NMR software |
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| Refinement | Method: TORSION ANGLE DYNAMICS, SIMULATED ANNEALING / Software ordinal: 1 Details: THE STRUCTURES ARE BASED ON A TOTAL OF 2138 DISTANCE RESTRAINTS, INCLUDING 2062 NOE-DERIVED DISTANCE RESTRAINTS [1625 UNAMBIGUOUS AND 437 AMBIGUOUS RESTRAINTS], 76 HYDROGEN BONDING DISTANCE ...Details: THE STRUCTURES ARE BASED ON A TOTAL OF 2138 DISTANCE RESTRAINTS, INCLUDING 2062 NOE-DERIVED DISTANCE RESTRAINTS [1625 UNAMBIGUOUS AND 437 AMBIGUOUS RESTRAINTS], 76 HYDROGEN BONDING DISTANCE RESTRAINTS, AND 112 TORSION ANGLE RESTRAINTS. | ||||||||||||||||||||
| NMR representative | Selection criteria: closest to the average | ||||||||||||||||||||
| NMR ensemble | Conformer selection criteria: The submitted conformers are the 20 structures with the lowest restraint energies, restraint violations, and RMS deviations from ideal covalent geometry Conformers calculated total number: 80 / Conformers submitted total number: 20 |
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