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Yorodumi- PDB-9jtl: Human glucose 6 phosphate catalytic subunit 1 (hG6PC1) in apo state. -
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Open data
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Basic information
| Entry | Database: PDB / ID: 9jtl | ||||||
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| Title | Human glucose 6 phosphate catalytic subunit 1 (hG6PC1) in apo state. | ||||||
Components | Glucose-6-phosphatase catalytic subunit 1,GS linker-HRV3C-GFP-twin strep | ||||||
Keywords | HYDROLASE / membrane protein / glucose metabolism | ||||||
| Function / homology | Function and homology informationglucose-6-phosphatase / Glycogen storage disease type Ia (G6PC) / glucose-6-phosphatase activity / glucose-6-phosphate transport / phosphotransferase activity, alcohol group as acceptor / response to resveratrol / urate metabolic process / glucose 6-phosphate metabolic process / Gluconeogenesis / response to carbohydrate ...glucose-6-phosphatase / Glycogen storage disease type Ia (G6PC) / glucose-6-phosphatase activity / glucose-6-phosphate transport / phosphotransferase activity, alcohol group as acceptor / response to resveratrol / urate metabolic process / glucose 6-phosphate metabolic process / Gluconeogenesis / response to carbohydrate / glycogen catabolic process / triglyceride metabolic process / response to food / glycogen metabolic process / phosphate ion binding / steroid metabolic process / FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes / cholesterol homeostasis / gluconeogenesis / multicellular organism growth / cellular response to insulin stimulus / glucose homeostasis / regulation of gene expression / endoplasmic reticulum membrane / membrane Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.4 Å | ||||||
Authors | Chen, Q. / Zhao, Y. / Wang, Y. | ||||||
| Funding support | China, 1items
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Citation | Journal: Cell Discov / Year: 2025Title: The induced-fit and catalytic mechanisms of human G6PC1. Authors: Qihao Chen / Yuhang Wang / Renjie Li / Qinru Bai / Yan Zhao / ![]() Abstract: Human glucose-6-phosphatase catalytic subunit 1 (hG6PC1) is a key enzyme in glucose metabolism, governing the final common step of gluconeogenesis and glycogenolysis, and directly regulating energy ...Human glucose-6-phosphatase catalytic subunit 1 (hG6PC1) is a key enzyme in glucose metabolism, governing the final common step of gluconeogenesis and glycogenolysis, and directly regulating energy homeostasis. Aberrant mutations in G6PC1 directly cause glycogen storage disease type 1a, which is characterized by chronic hypoglycemia and glycogen accumulation. Additionally, abnormal G6PC1 function leads to increased fasting blood glucose. Consequently, it is a critical target for treating glucose metabolism disorders. In this study, we determine the cryo-EM structures of G6PC1 in both the partially open and fully open states, in either the apo form or in complex with the substrates G6P or F6P and the product phosphate. These structures offer distinct insights into the mechanism of hydrolysis and induced-fit, providing a structural foundation for the diagnostic analysis of disease-causing mutations in G6PC1. Moreover, we propose a potential mechanism by which phosphatidylserine regulates G6PC1 activity, providing a novel perspective on its role and implications. | ||||||
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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 | 9jtl.cif.gz | 80 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9jtl.ent.gz | 54.9 KB | Display | PDB format |
| PDBx/mmJSON format | 9jtl.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 9jtl_validation.pdf.gz | 1.5 MB | Display | wwPDB validaton report |
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| Full document | 9jtl_full_validation.pdf.gz | 1.5 MB | Display | |
| Data in XML | 9jtl_validation.xml.gz | 24.7 KB | Display | |
| Data in CIF | 9jtl_validation.cif.gz | 33.2 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/jt/9jtl ftp://data.pdbj.org/pub/pdb/validation_reports/jt/9jtl | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 61811MC ![]() 9jtmC ![]() 9jtnC ![]() 9jtoC 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: 71901.078 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Details: hG6PC1-GS linker-HRV3C-GFP-twin strep / Source: (gene. exp.) Homo sapiens (human) / Gene: G6PC1, G6PC, G6PT / Production host: Homo sapiens (human) / References: UniProt: P35575, glucose-6-phosphatase |
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| #2: Chemical | ChemComp-P5S / |
| Has ligand of interest | Y |
| Has protein modification | Y |
-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: Glucose 6 phosphate catalytic subunit 1 / Type: COMPLEX / Entity ID: #1 / Source: RECOMBINANT |
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| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | 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 |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TALOS ARCTICA |
| 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: 1200 nm |
| Image recording | Electron dose: 60 e/Å2 / Film or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: PHASE FLIPPING ONLY | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 3.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 28471 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi



Homo sapiens (human)
China, 1items
Citation






PDBj











FIELD EMISSION GUN