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Open data
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Basic information
Entry | Database: PDB / ID: 8j7o | ||||||
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Title | Human pyruvate carboxylase in BCCP-CTS state without BC | ||||||
![]() | Pyruvate carboxylase, mitochondrial | ||||||
![]() | CYTOSOLIC PROTEIN / PC / Mitochondrial | ||||||
Function / homology | ![]() Defective HLCS causes multiple carboxylase deficiency / pyruvate carboxylase / pyruvate carboxylase activity / Biotin transport and metabolism / viral RNA genome packaging / NADP metabolic process / positive regulation by host of viral process / Pyruvate metabolism / Gluconeogenesis / NADH metabolic process ...Defective HLCS causes multiple carboxylase deficiency / pyruvate carboxylase / pyruvate carboxylase activity / Biotin transport and metabolism / viral RNA genome packaging / NADP metabolic process / positive regulation by host of viral process / Pyruvate metabolism / Gluconeogenesis / NADH metabolic process / pyruvate metabolic process / biotin binding / viral release from host cell / gluconeogenesis / lipid metabolic process / mitochondrial matrix / negative regulation of gene expression / mitochondrion / ATP binding / identical protein binding / metal ion binding / cytosol / cytoplasm Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.83 Å | ||||||
![]() | Liu, D.S. / Su, J.Y. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Human pyruvate carboxylase Authors: Liu, D.S. / Su, J.Y. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 496.2 KB | Display | ![]() |
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PDB format | ![]() | 388.1 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Arichive directory | ![]() ![]() | HTTPS FTP |
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-Related structure data
Related structure data | ![]() 36044MC 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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1 |
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Components
#1: Protein | Mass: 129799.359 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() #2: Chemical | ChemComp-BTI / Has ligand of interest | Y | |
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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: Tetramer complex of human pyruvate carboxylase / Type: COMPLEX / Entity ID: #1 / 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 ONLY |
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3D reconstruction | Resolution: 3.83 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 21326 / Symmetry type: POINT |