+Open data
-Basic information
Entry | Database: PDB / ID: 9ayb | ||||||||||||
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Title | Structure of Apo Sialin S61A mutant | ||||||||||||
Components | Sialin | ||||||||||||
Keywords | MEMBRANE PROTEIN / Transporter | ||||||||||||
Function / homology | Function and homology information sialic acid:proton symporter activity / D-glucuronate transmembrane transporter activity / Defective SLC17A5 causes Salla disease (SD) and ISSD / Organic anion transporters / sialic acid transmembrane transporter activity / sialic acid transport / carbohydrate:proton symporter activity / Sialic acid metabolism / monoatomic anion transport / amino acid transport ...sialic acid:proton symporter activity / D-glucuronate transmembrane transporter activity / Defective SLC17A5 causes Salla disease (SD) and ISSD / Organic anion transporters / sialic acid transmembrane transporter activity / sialic acid transport / carbohydrate:proton symporter activity / Sialic acid metabolism / monoatomic anion transport / amino acid transport / monoatomic ion transport / response to bacterium / synaptic vesicle membrane / basolateral plasma membrane / lysosome / lysosomal membrane / membrane / plasma membrane / cytosol Similarity search - Function | ||||||||||||
Biological species | Homo sapiens (human) | ||||||||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.19 Å | ||||||||||||
Authors | Schmiege, P. / Li, X. | ||||||||||||
Funding support | United States, 3items
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Citation | Journal: To Be Published Title: Structure of Apo Sialin S61A mutant Authors: Schmiege, P. / Li, X. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 9ayb.cif.gz | 94.4 KB | Display | PDBx/mmCIF format |
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PDB format | pdb9ayb.ent.gz | 70.1 KB | Display | PDB format |
PDBx/mmJSON format | 9ayb.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 9ayb_validation.pdf.gz | 1.4 MB | Display | wwPDB validaton report |
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Full document | 9ayb_full_validation.pdf.gz | 1.4 MB | Display | |
Data in XML | 9ayb_validation.xml.gz | 25 KB | Display | |
Data in CIF | 9ayb_validation.cif.gz | 33.3 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ay/9ayb ftp://data.pdbj.org/pub/pdb/validation_reports/ay/9ayb | HTTPS FTP |
-Related structure data
Related structure data | 43984MC M: map data used to model this data C: citing same article (ref.) |
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Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
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1 |
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-Components
#1: Protein | Mass: 55665.137 Da / Num. of mol.: 1 / Mutation: S61A Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: SLC17A5 / Production host: Homo sapiens (human) / References: UniProt: Q9NRA2 |
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-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
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EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Structure of Apo Sialin S61A mutant / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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Source (natural) | Organism: Homo sapiens (human) |
Source (recombinant) | Organism: Homo sapiens (human) |
Buffer solution | pH: 7.5 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
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Microscopy | Model: FEI TITAN 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: 60 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k) |
-Processing
CTF correction | Type: NONE |
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3D reconstruction | Resolution: 3.19 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 199874 / Symmetry type: POINT |