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Open data
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Basic information
Entry | Database: PDB / ID: 5ezb | |||||||||
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Title | Chicken prestin STAS domain | |||||||||
![]() | Chicken prestin STAS domain,Chicken prestin STAS domain | |||||||||
![]() | TRANSPORT PROTEIN / Eukaryotic SLC26 STAS fold | |||||||||
Function / homology | ![]() : / lateral wall of outer hair cell / sulfate transmembrane transporter activity / secondary active sulfate transmembrane transporter activity / oxalate transmembrane transporter activity / bicarbonate transmembrane transporter activity / chloride transmembrane transporter activity / spectrin binding / plasma membrane => GO:0005886 / lateral plasma membrane ...: / lateral wall of outer hair cell / sulfate transmembrane transporter activity / secondary active sulfate transmembrane transporter activity / oxalate transmembrane transporter activity / bicarbonate transmembrane transporter activity / chloride transmembrane transporter activity / spectrin binding / plasma membrane => GO:0005886 / lateral plasma membrane / regulation of membrane potential / sensory perception of sound / basolateral plasma membrane / metal ion binding Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | ![]() ![]() ![]() | |||||||||
![]() | Lolli, G. / Pasqualetto, E. / Costanzi, E. / Bonetto, G. / Battistutta, R. | |||||||||
Funding support | ![]()
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![]() | ![]() Title: The STAS domain of mammalian SLC26A5 prestin harbours an anion-binding site. Authors: Lolli, G. / Pasqualetto, E. / Costanzi, E. / Bonetto, G. / Battistutta, R. #1: ![]() Title: Structure of the cytosolic portion of the motor protein prestin and functional role of the STAS domain in SLC26/SulP anion transporters. Authors: Pasqualetto, E. / Aiello, R. / Gesiot, L. / Bonetto, G. / Bellanda, M. / Battistutta, R. | |||||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 114.4 KB | Display | ![]() |
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PDB format | ![]() | 89.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 453.1 KB | Display | ![]() |
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Full document | ![]() | 455 KB | Display | |
Data in XML | ![]() | 12.6 KB | Display | |
Data in CIF | ![]() | 16.6 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5eusC ![]() 5euuC ![]() 5euwC ![]() 5euxC ![]() 5euzC ![]() 3lloS S: Starting model for refinement C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 | ![]()
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2 | ![]()
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 1 / Ens-ID: 1 / Beg auth comp-ID: GLN / Beg label comp-ID: GLN / End auth comp-ID: GLY / End label comp-ID: GLY / Auth seq-ID: 513 - 730 / Label seq-ID: 3 - 140
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Components
-Protein , 1 types, 2 molecules AB
#1: Protein | Mass: 15982.049 Da / Num. of mol.: 2 / Fragment: STAS domain,STAS domain Mutation: Residues 570-651 (variable loop) are deleted, GlySer are inserted between position 569 and 652,Residues 570-651 (variable loop) are deleted, GlySer are inserted between position 569 and 652 Source method: isolated from a genetically manipulated source Details: Residues 570-651 (variable loop) are deleted, GlySer are inserted between position 569 and 652 Source: (gene. exp.) ![]() ![]() ![]() ![]() |
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-Non-polymers , 5 types, 59 molecules ![](data/chem/img/ZN.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/OXL.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/GOL.gif)
![](data/chem/img/NA.gif)
![](data/chem/img/OXL.gif)
![](data/chem/img/HOH.gif)
#2: Chemical | #3: Chemical | ChemComp-GOL / | #4: Chemical | ChemComp-NA / | #5: Chemical | ChemComp-OXL / | #6: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 3.81 Å3/Da / Density % sol: 67.69 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 0.1 M Tris pH 8.5, 1.5 M Ammonium Sulphate, 12% (v/v) glycerol, 0.3 M Ammonium oxalate |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 2M / Detector: PIXEL / Date: Oct 23, 2013 |
Radiation | Monochromator: Si(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.91 Å / Relative weight: 1 |
Reflection | Resolution: 2.3→46.59 Å / Num. obs: 19970 / % possible obs: 96.1 % / Redundancy: 6.4 % / Rmerge(I) obs: 0.069 / Net I/σ(I): 18.9 |
Reflection shell | Resolution: 2.3→2.38 Å / Redundancy: 6.3 % / Rmerge(I) obs: 0.665 / Mean I/σ(I) obs: 2.8 / % possible all: 96.9 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 3LLO Resolution: 2.3→46.585 Å / SU ML: 0.27 / Cross valid method: FREE R-VALUE / σ(F): 1.33 / Phase error: 30.08 / Stereochemistry target values: ML
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Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso max: 151.58 Å2 / Biso mean: 55.1761 Å2 / Biso min: 28.72 Å2 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Refinement step | Cycle: final / Resolution: 2.3→46.585 Å
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Refine LS restraints |
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Refine LS restraints NCS |
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LS refinement shell |
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