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Open data
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Basic information
| Entry | Database: PDB / ID: 9lgy | |||||||||||||||||||||
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| Title | Cryo-EM structure of CsKCS6-CsCER2 like1 complex | |||||||||||||||||||||
Components |
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Keywords | PLANT PROTEIN / CsKCS6-CsCER2 like1 complex | |||||||||||||||||||||
| Function / homology | Function and homology informationfatty acid elongase activity / Transferases; Acyltransferases; Transferring groups other than aminoacyl groups / fatty acid biosynthetic process / membrane Similarity search - Function | |||||||||||||||||||||
| Biological species | ![]() | |||||||||||||||||||||
| Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.4 Å | |||||||||||||||||||||
Authors | Wang, Y. / Guan, Z.Y. / Zhu, F. / Chen, Y.J. / Yin, P. | |||||||||||||||||||||
| Funding support | China, 1items
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Citation | Journal: To Be PublishedTitle: structural basis for Synthesis of long-chain fatty acids Authors: Wang, Y. / Yin, P. | |||||||||||||||||||||
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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 | 9lgy.cif.gz | 587.5 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb9lgy.ent.gz | 488.9 KB | Display | PDB format |
| PDBx/mmJSON format | 9lgy.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/lg/9lgy ftp://data.pdbj.org/pub/pdb/validation_reports/lg/9lgy | HTTPS FTP |
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-Related structure data
| Related structure data | ![]() 63076MC ![]() 9kqgC 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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| 1 |
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Components
| #1: Protein | Mass: 50863.973 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Homo sapiens (human)#2: Protein | Mass: 59652.207 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Homo sapiens (human)References: UniProt: A0A067FRD2, Transferases; Acyltransferases; Transferring groups other than aminoacyl groups #3: Chemical | ChemComp-D12 / | #4: Chemical | ChemComp-R16 / | Has ligand of interest | N | 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: CsKCS2-CsCER2 like1 complex / Type: COMPLEX / Entity ID: #1-#2 / Source: MULTIPLE SOURCES |
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| Source (natural) | Organism: ![]() |
| 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: 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: BRIGHT FIELD / Nominal defocus max: 1600 nm / Nominal defocus min: 1200 nm |
| Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) |
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Processing
| EM software | Name: PHENIX / Version: 1.21.2_5419 / Category: model refinement | ||||||||||||||||||||||||
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| CTF correction | Type: NONE | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 2.4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 272363 / Symmetry type: POINT | ||||||||||||||||||||||||
| Refinement | Highest resolution: 2.4 Å Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS) | ||||||||||||||||||||||||
| Refine LS restraints |
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About Yorodumi






China, 1items
Citation


PDBj


Homo sapiens (human)


FIELD EMISSION GUN