+
Open data
-
Basic information
| Entry | Database: PDB / ID: 31ew | |||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Title | UapA (WT) in DDM, Apo state | |||||||||||||||||||||||||||||||||
Components | Uric acid-xanthine permease | |||||||||||||||||||||||||||||||||
Keywords | MEMBRANE PROTEIN / UapA / DDM / Transporter / Inward-facing / Uric Acid / Xanthine | |||||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationxanthine transport / xanthine transmembrane transporter activity / autophagosome lumen / purine nucleobase binding / urate transport / urate transmembrane transporter activity / fungal-type vacuole / endosome membrane / plasma membrane Similarity search - Function | |||||||||||||||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.06 Å | |||||||||||||||||||||||||||||||||
Authors | Broutzakis, G. / Gatsogiannis, C. | |||||||||||||||||||||||||||||||||
| Funding support | Germany, 2items
| |||||||||||||||||||||||||||||||||
Citation | Journal: To Be PublishedTitle: Cryo-EM of the eukaryotic purine transporter UapA demonstrates intramolecular and lipid regulation of transport Authors: Broutzakis, G. / Pyrris, Y. / Akrani, I. / Neuhaus, A. / Mikros, E. / Diallinas, G. / Gatsogiannis, C. | |||||||||||||||||||||||||||||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 31ew.cif.gz | 251.3 KB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb31ew.ent.gz | 202.8 KB | Display | PDB format |
| PDBx/mmJSON format | 31ew.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/1e/31ew ftp://data.pdbj.org/pub/pdb/validation_reports/1e/31ew | HTTPS FTP |
|---|
-Related structure data
| Related structure data | ![]() 58351 ![]() 31eyC ![]() 31ezC M: map data used to model this data C: citing same article ( |
|---|---|
| Similar structure data | Similarity search - Function & homology F&H Search |
-
Links
-
Assembly
| Deposited unit | ![]()
|
|---|---|
| 1 |
|
-
Components
-Protein / Sugars , 2 types, 16 molecules AB

| #1: Protein | Mass: 60291.586 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Sugar | ChemComp-LMT / |
|---|
-Non-polymers , 6 types, 458 molecules 










| #3: Chemical | ChemComp-MYR / #4: Chemical | ChemComp-PLM / #5: Chemical | ChemComp-ERG / #6: Chemical | ChemComp-DAO / #7: Chemical | ChemComp-DGA / #8: Water | ChemComp-HOH / | |
|---|
-Details
| Has ligand of interest | N |
|---|---|
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
|---|---|
| EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-
Sample preparation
| Component | Name: UapA (WT) in DDM, Apo state / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT | ||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Molecular weight | Value: 0.12 MDa / Experimental value: NO | ||||||||||||||||||||
| Source (natural) | Organism: ![]() | ||||||||||||||||||||
| Source (recombinant) | Organism: ![]() | ||||||||||||||||||||
| Buffer solution | pH: 7.5 | ||||||||||||||||||||
| Buffer component |
| ||||||||||||||||||||
| Specimen | Conc.: 5 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES | ||||||||||||||||||||
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 286.15 K Details: Vitrification chamber was allowed to equilibrate for 15 min at 100% humidity. |
-
Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
|---|---|
| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2200 nm / Nominal defocus min: 800 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
-
Processing
| EM software |
| ||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.06 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 499617 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 2.06 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
|
Movie
Controller
About Yorodumi






Germany, 2items
Citation


PDBj












FIELD EMISSION GUN