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- PDB-7vzr: Structure of the Acidobacteria homodimeric reaction center bound ... -
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Open data
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Basic information
Entry | Database: PDB / ID: 7vzr | ||||||
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Title | Structure of the Acidobacteria homodimeric reaction center bound with cytochrome c (the smaller form) | ||||||
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![]() | PHOTOSYNTHESIS / membrane protein | ||||||
Function / homology | ![]() thylakoid / photosynthesis / electron transfer activity / iron ion binding / heme binding / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.22 Å | ||||||
![]() | Huang, G.Q. / Dong, S.S. / Qin, X.C. / Sui, S.F. | ||||||
Funding support | 1items
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![]() | ![]() Title: Structure of the Acidobacteria homodimeric reaction center bound with cytochrome c Authors: Dong, S. / Huang, G. / Wang, C. / Wang, J. / Sui, S.F. / Qin, X. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 484.5 KB | Display | ![]() |
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PDB format | ![]() | 381.2 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 2.9 MB | Display | ![]() |
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Full document | ![]() | 3.2 MB | Display | |
Data in XML | ![]() | 108.3 KB | Display | |
Data in CIF | ![]() | 146 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 32229MC 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
-Protein , 3 types, 4 molecules AaCc
#1: Protein | Mass: 99311.414 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: G2LDR8 #2: Protein | | Mass: 24138.053 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: G2LDR4 #7: Protein | | Mass: 15664.669 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: G2LDR3 |
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-Protein/peptide , 4 types, 8 molecules EeFfGgHh
#3: Protein/peptide | Mass: 3684.458 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: G2LK98 #4: Protein/peptide | Mass: 3885.684 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: G2LEN5 #5: Protein/peptide | Mass: 5041.152 Da / Num. of mol.: 2 / Source method: isolated from a natural source Source: (natural) ![]() References: UniProt: G2LJ20 #6: Protein/peptide | Mass: 1635.006 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Production host: ![]() ![]() |
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-Non-polymers , 12 types, 85 molecules ![](data/chem/img/2GO.gif)
![](data/chem/img/BCL.gif)
![](data/chem/img/CLA.gif)
![](data/chem/img/LYC.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/85I.gif)
![](data/chem/img/85N.gif)
![](data/chem/img/HEC.gif)
![](data/chem/img/84Q.gif)
![](data/chem/img/SF4.gif)
![](data/chem/img/HOH.gif)
![](data/chem/img/BCL.gif)
![](data/chem/img/CLA.gif)
![](data/chem/img/LYC.gif)
![](data/chem/img/CA.gif)
![](data/chem/img/85I.gif)
![](data/chem/img/85N.gif)
![](data/chem/img/HEC.gif)
![](data/chem/img/84Q.gif)
![](data/chem/img/SF4.gif)
![](data/chem/img/HOH.gif)
#8: Chemical | #9: Chemical | ChemComp-BCL / #10: Chemical | ChemComp-CLA / #11: Chemical | #12: Chemical | #13: Chemical | ChemComp-85I / [( #14: Chemical | ChemComp-UNL / Mass: 671.023 Da / Num. of mol.: 32 / Source method: obtained synthetically / Feature type: SUBJECT OF INVESTIGATION #15: Chemical | ChemComp-85N / [( #16: Chemical | #17: Chemical | #18: Chemical | ChemComp-SF4 / | #19: Water | ChemComp-HOH / | |
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-Details
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: CabRC complex / Type: COMPLEX / Entity ID: #1-#7 / Source: NATURAL |
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Source (natural) | Organism: ![]() |
Buffer solution | pH: 7.6 |
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: 2000 nm / Nominal defocus min: 500 nm / Cs: 2.7 mm |
Image recording | Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
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Processing
CTF correction | Type: NONE |
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3D reconstruction | Resolution: 2.22 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 490075 / Symmetry type: POINT |
Refinement | Highest resolution: 2.22 Å |