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Open data
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Basic information
Entry | Database: PDB / ID: 7blz | ||||||
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Title | Red alga C.merolae Photosystem I | ||||||
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![]() | PHOTOSYNTHESIS / Red alga C.merolae Photosystem I | ||||||
Function / homology | ![]() plastid thylakoid membrane / thylakoid membrane / photosynthesis, light harvesting / photosystem I reaction center / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / photosystem II / chlorophyll binding / chloroplast thylakoid membrane ...plastid thylakoid membrane / thylakoid membrane / photosynthesis, light harvesting / photosystem I reaction center / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / photosystem II / chlorophyll binding / chloroplast thylakoid membrane / photosynthesis / chloroplast / 4 iron, 4 sulfur cluster binding / oxidoreductase activity / electron transfer activity / magnesium ion binding / membrane / metal ion binding Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.1 Å | ||||||
![]() | Nelson, N. / Klaiman, D. / Hippler, M. | ||||||
Funding support | ![]()
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![]() | ![]() Title: Red alga C.merolae Photosystem I Authors: Nelson, N. / Klaiman, D. / Hippler, M. | ||||||
History |
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Structure visualization
Movie |
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Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 1.4 MB | Display | ![]() |
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PDB format | ![]() | 1.3 MB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 12.7 MB | Display | ![]() |
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Full document | ![]() | 13.3 MB | Display | |
Data in XML | ![]() | 215.4 KB | Display | |
Data in CIF | ![]() | 261.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 12228MC M: map data used to model this data C: citing same article ( |
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Similar structure data |
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Links
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Assembly
Deposited unit | ![]()
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1 |
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Components
-Protein , 6 types, 6 molecules 123FKO
#1: Protein | Mass: 19551.574 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: 10D / References: UniProt: M1VKK5 |
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#2: Protein | Mass: 19796.850 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: 10D / References: UniProt: M1UU36 |
#3: Protein | Mass: 19041.045 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: 10D |
#9: Protein | Mass: 17997.396 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: 10D / References: UniProt: A0A5P9RU83 |
#12: Protein | Mass: 5608.732 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: 10D / References: UniProt: Q85G51 |
#15: Protein | Mass: 10485.055 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: 10D / References: UniProt: M1VFJ4 |
-Photosystem I P700 chlorophyll a apoprotein ... , 3 types, 3 molecules ABD
#4: Protein | Mass: 82215.789 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: 10D / References: UniProt: Q85FY7, photosystem I |
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#5: Protein | Mass: 81976.656 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: 10D / References: UniProt: Q85FY6, photosystem I |
#7: Protein | Mass: 15567.736 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: 10D / References: UniProt: Q85FY0 |
-Photosystem I iron-sulfur ... , 2 types, 2 molecules CE
#6: Protein | Mass: 8691.076 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: 10D / References: UniProt: Q85G47, photosystem I |
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#8: Protein | Mass: 6985.040 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: 10D / References: UniProt: Q85FZ1 |
-Photosystem I reaction center subunit ... , 4 types, 4 molecules IJLM
#10: Protein/peptide | Mass: 3276.988 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: 10D / References: UniProt: Q85FQ6 |
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#11: Protein/peptide | Mass: 4410.245 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: 10D / References: UniProt: A0A5P9RTH6 |
#13: Protein | Mass: 14690.970 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: 10D / References: UniProt: Q85FP8 |
#14: Protein/peptide | Mass: 2937.604 Da / Num. of mol.: 1 / Source method: isolated from a natural source Source: (natural) ![]() Strain: 10D / References: UniProt: Q85G73 |
-Sugars , 2 types, 5 molecules 


#24: Sugar | #31: Sugar | |
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-Non-polymers , 16 types, 450 molecules 






























#16: Chemical | ChemComp-CLA / #17: Chemical | ChemComp-C7Z / ( #18: Chemical | ChemComp-RRX / ( #19: Chemical | ChemComp-LHG / #20: Chemical | #21: Chemical | ChemComp-BCR / #22: Chemical | #23: Chemical | #25: Chemical | ChemComp-PTY / #26: Chemical | ChemComp-CL0 / | #27: Chemical | #28: Chemical | #29: Chemical | #30: Chemical | ChemComp-T7X / | #32: Chemical | #33: Water | ChemComp-HOH / | |
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-Details
Has ligand of interest | N |
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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: Photosystem I / Type: COMPLEX / Entity ID: #1-#15 / 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 |
Specimen support | Grid material: COPPER / Grid type: Quantifoil R1.2/1.3 |
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 |
Image recording | Electron dose: 40 e/Å2 / Film or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Num. of real images: 7220 |
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Processing
Software | Name: PHENIX / Version: 1.19_4092: / Classification: refinement | ||||||||||||||||||||||||||||||||
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EM software |
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CTF correction | Type: NONE | ||||||||||||||||||||||||||||||||
Particle selection | Num. of particles selected: 1198564 | ||||||||||||||||||||||||||||||||
3D reconstruction | Resolution: 3.1 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 128943 / Num. of class averages: 8 / Symmetry type: POINT | ||||||||||||||||||||||||||||||||
Atomic model building | Protocol: RIGID BODY FIT / Space: REAL | ||||||||||||||||||||||||||||||||
Refinement | Cross valid method: NONE Stereochemistry target values: GeoStd + Monomer Library + CDL v1.2 | ||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 35.12 Å2 | ||||||||||||||||||||||||||||||||
Refine LS restraints |
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