+Open data
-Basic information
Entry | Database: PDB / ID: 8j7o | ||||||
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Title | Human pyruvate carboxylase in BCCP-CTS state without BC | ||||||
Components | Pyruvate carboxylase, mitochondrial | ||||||
Keywords | CYTOSOLIC PROTEIN / PC / Mitochondrial | ||||||
Function / homology | Function and homology information 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 / Gluconeogenesis / NADH metabolic process / pyruvate 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 / 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 / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.83 Å | ||||||
Authors | Liu, D.S. / Su, J.Y. | ||||||
Funding support | China, 1items
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Citation | Journal: To Be Published Title: Human pyruvate carboxylase Authors: Liu, D.S. / Su, J.Y. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 8j7o.cif.gz | 496.2 KB | Display | PDBx/mmCIF format |
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PDB format | pdb8j7o.ent.gz | 388.1 KB | Display | PDB format |
PDBx/mmJSON format | 8j7o.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 8j7o_validation.pdf.gz | 1.7 MB | Display | wwPDB validaton report |
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Full document | 8j7o_full_validation.pdf.gz | 1.7 MB | Display | |
Data in XML | 8j7o_validation.xml.gz | 76.9 KB | Display | |
Data in CIF | 8j7o_validation.cif.gz | 116.7 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/j7/8j7o ftp://data.pdbj.org/pub/pdb/validation_reports/j7/8j7o | HTTPS FTP |
-Related structure data
Related structure data | 36044MC 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: 129799.359 Da / Num. of mol.: 4 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PC / Production host: Homo sapiens (human) / References: UniProt: P11498, pyruvate carboxylase #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 |
-Sample preparation
Component | Name: Tetramer complex of human pyruvate carboxylase / Type: COMPLEX / Entity ID: #1 / Source: NATURAL |
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Source (natural) | Organism: Homo sapiens (human) |
Buffer solution | pH: 8 |
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: 1800 nm / Nominal defocus min: 1300 nm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-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 |