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Open data
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Basic information
Entry | Database: PDB / ID: 7ybu | ||||||
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Title | Human propionyl-coenzyme A carboxylase | ||||||
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![]() | CYTOSOLIC PROTEIN / Cryo-EM / PCC / Mitochondria | ||||||
Function / homology | ![]() short-chain fatty acid catabolic process / branched-chain amino acid metabolic process / Propionyl-CoA catabolism / propionyl-CoA carboxylase / urea carboxylase activity / propionyl-CoA carboxylase activity / Defective HLCS causes multiple carboxylase deficiency / methylcrotonoyl-CoA carboxylase activity / Biotin transport and metabolism / biotin binding ...short-chain fatty acid catabolic process / branched-chain amino acid metabolic process / Propionyl-CoA catabolism / propionyl-CoA carboxylase / urea carboxylase activity / propionyl-CoA carboxylase activity / Defective HLCS causes multiple carboxylase deficiency / methylcrotonoyl-CoA carboxylase activity / Biotin transport and metabolism / biotin binding / catalytic complex / fatty acid metabolic process / mitochondrial matrix / enzyme binding / mitochondrion / ATP binding / metal ion binding / cytosol Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.2 Å | ||||||
![]() | Su, J.Y. / Liu, D.S. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Human propionyl-coenzyme A carboxylase Authors: Su, J.Y. / Liu, D.S. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.1 MB | Display | ![]() |
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PDB format | ![]() | 975.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 1.3 MB | Display | ![]() |
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Full document | ![]() | 1.4 MB | Display | |
Data in XML | ![]() | 178.2 KB | Display | |
Data in CIF | ![]() | 276.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 33729MC M: map data used to model this data C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
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Assembly
Deposited unit | ![]()
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Components
#1: Protein | Mass: 80161.922 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #2: Protein | Mass: 58284.488 Da / Num. of mol.: 6 / Source method: isolated from a natural source / Source: (natural) ![]() #3: Chemical | ChemComp-BTI / Has ligand of interest | 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: Human propionyl-coenzyme A carboxylase heterododecomer Type: COMPLEX / Entity ID: #1-#2 / Source: NATURAL |
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Source (natural) | Organism: ![]() |
Buffer solution | pH: 8 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Vitrification | Cryogen name: ETHANE |
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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: ![]() |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 1800 nm / Nominal defocus min: 1300 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
CTF correction | Type: PHASE FLIPPING AND AMPLITUDE CORRECTION |
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3D reconstruction | Resolution: 2.2 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 99377 / Symmetry type: POINT |