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Open data
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Basic information
| Entry | Database: PDB / ID: 9ngj | ||||||||||||||||||||||||||||||
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| Title | CryoEM structure of human ABCD3 bound to Phytanoyl-CoA | ||||||||||||||||||||||||||||||
Components | ATP-binding cassette sub-family D member 3 | ||||||||||||||||||||||||||||||
Keywords | TRANSPORT PROTEIN / ABC transporter / Peroxisome / Fatty-acid transport | ||||||||||||||||||||||||||||||
| Function / homology | Function and homology informationphytanic acid metabolic process / long-chain fatty acid import into peroxisome / very long-chain fatty acid catabolic process / very long-chain fatty acid metabolic process / Class I peroxisomal membrane protein import / peroxisome organization / fatty acyl-CoA hydrolase activity / ABC transporters in lipid homeostasis / bile acid biosynthetic process / Hydrolases; Acting on ester bonds; Thioester hydrolases ...phytanic acid metabolic process / long-chain fatty acid import into peroxisome / very long-chain fatty acid catabolic process / very long-chain fatty acid metabolic process / Class I peroxisomal membrane protein import / peroxisome organization / fatty acyl-CoA hydrolase activity / ABC transporters in lipid homeostasis / bile acid biosynthetic process / Hydrolases; Acting on ester bonds; Thioester hydrolases / Translocases; Catalysing the translocation of other compounds; Linked to the hydrolysis of a nucleoside triphosphate / peroxisomal membrane / long-chain fatty acid transmembrane transporter activity / bile acid and bile salt transport / fatty acid beta-oxidation / RHOC GTPase cycle / peroxisomal matrix / RHOA GTPase cycle / ATPase-coupled transmembrane transporter activity / ABC-type transporter activity / fatty acid biosynthetic process / peroxisome / response to xenobiotic stimulus / intracellular membrane-bounded organelle / protein homodimerization activity / ATP hydrolysis activity / mitochondrion / ATP binding / membrane / cytosol Similarity search - Function | ||||||||||||||||||||||||||||||
| Biological species | Homo sapiens (human) | ||||||||||||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.13 Å | ||||||||||||||||||||||||||||||
Authors | Gupta, M. / Khandelwal, N.K. / Stroud, R.M. | ||||||||||||||||||||||||||||||
| Funding support | United States, 1items
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Citation | Journal: To Be PublishedTitle: Structural analysis of a human peroxisomal fatty-acid transporter Authors: Gupta, M. / Khandelwal, N.K. / Stroud, R.M. | ||||||||||||||||||||||||||||||
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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 | 9ngj.cif.gz | 460.7 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9ngj.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 9ngj.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9ngj_validation.pdf.gz | 1.3 MB | Display | wwPDB validaton report |
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| Full document | 9ngj_full_validation.pdf.gz | 1.3 MB | Display | |
| Data in XML | 9ngj_validation.xml.gz | 52.1 KB | Display | |
| Data in CIF | 9ngj_validation.cif.gz | 75 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ng/9ngj ftp://data.pdbj.org/pub/pdb/validation_reports/ng/9ngj | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 49386MC ![]() 9ngmC M: map data used to model this data C: citing same article ( |
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| Similar structure data | Similarity search - Function & homology F&H Search |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 78243.727 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Details: ABCD3-thrombin_cleavage_site-GS_linker-8XHis_tag / Source: (gene. exp.) Homo sapiens (human) / Gene: ABCD3, PMP70, PXMP1 / Production host: ![]() References: UniProt: P28288, Hydrolases; Acting on ester bonds; Thioester hydrolases, Translocases; Catalysing the translocation of other compounds; Linked to the hydrolysis of a nucleoside triphosphate #2: Chemical | Mass: 1062.049 Da / Num. of mol.: 2 / Source method: obtained synthetically / Formula: C41H74N7O17P3S / Feature type: SUBJECT OF INVESTIGATION Has ligand of interest | Y | Has protein modification | N | |
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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 |
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Sample preparation
| Component | Name: ABCD3 dimer with Phytanoyl-CoA / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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| Molecular weight | Experimental value: NO |
| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: GOLD / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3 |
| Vitrification | Instrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 281.15 K |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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| Microscopy | Model: TFS KRIOS |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: OTHER / Nominal defocus max: 2 nm / Nominal defocus min: 1 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm |
| Image recording | Average exposure time: 2 sec. / Electron dose: 48 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 |
| Image scans | Sampling size: 5 µm |
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Processing
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| CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||
| 3D reconstruction | Resolution: 3.13 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 283849 / Symmetry type: POINT | ||||||||||||||||
| Refinement | Highest resolution: 3.13 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) |
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About Yorodumi




Homo sapiens (human)
United States, 1items
Citation


PDBj






FIELD EMISSION GUN