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Open data
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Basic information
| Entry | Database: PDB / ID: 2wsc | |||||||||||||||
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| Title | Improved Model of Plant Photosystem I | |||||||||||||||
Components |
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Keywords | PHOTOSYNTHESIS / ELECTRON TRANSFER / MEMBRANE PROTEINS / LARGE COMPLEXES | |||||||||||||||
| Function / homology | Function and homology informationchloroplast photosystem I / response to low light intensity stimulus / plastoglobule / response to high light intensity / chloroplast thylakoid / photosynthesis, light harvesting in photosystem I / thylakoid / photosynthesis, light harvesting / chloroplast thylakoid lumen / chloroplast envelope ...chloroplast photosystem I / response to low light intensity stimulus / plastoglobule / response to high light intensity / chloroplast thylakoid / photosynthesis, light harvesting in photosystem I / thylakoid / photosynthesis, light harvesting / chloroplast thylakoid lumen / chloroplast envelope / photosystem I reaction center / photosystem I / photosynthetic electron transport in photosystem I / photosystem I / photosystem II / chlorophyll binding / chloroplast thylakoid membrane / photosynthesis / response to cold / chloroplast / phosphoprotein binding / 4 iron, 4 sulfur cluster binding / molecular adaptor activity / oxidoreductase activity / electron transfer activity / protein domain specific binding / mRNA binding / magnesium ion binding / metal ion binding / plasma membrane Similarity search - Function | |||||||||||||||
| Biological species | ![]() PISUM SATIVUM (garden pea)![]() SPINACIA OLERACEA (spinach)![]() PHASEOLUS VULGARIS (common bean) | |||||||||||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.3 Å | |||||||||||||||
Authors | Amunts, A. / Toporik, H. / Borovikov, A. / Nelson, N. | |||||||||||||||
Citation | Journal: J.Biol.Chem. / Year: 2010Title: Structure Determination and Improved Model of Plant Photosystem I. Authors: Amunts, A. / Toporik, H. / Borovikova, A. / Nelson, N. | |||||||||||||||
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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 | 2wsc.cif.gz | 859.2 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb2wsc.ent.gz | 717.5 KB | Display | PDB format |
| PDBx/mmJSON format | 2wsc.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 2wsc_validation.pdf.gz | 64.1 MB | Display | wwPDB validaton report |
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| Full document | 2wsc_full_validation.pdf.gz | 65.4 MB | Display | |
| Data in XML | 2wsc_validation.xml.gz | 238.2 KB | Display | |
| Data in CIF | 2wsc_validation.cif.gz | 263 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/ws/2wsc ftp://data.pdbj.org/pub/pdb/validation_reports/ws/2wsc | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 2wseC ![]() 2wsfC ![]() 3lw5C ![]() 1yo9S C: citing same article ( S: Starting model for refinement |
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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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| Unit cell |
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Components
-Protein , 5 types, 5 molecules 1234C
| #1: Protein | Mass: 26021.895 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
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| #2: Protein | Mass: 28926.746 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) PISUM SATIVUM (garden pea) / References: UniProt: Q41038 |
| #3: Protein | Mass: 29852.055 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #4: Protein | Mass: 27181.982 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) PISUM SATIVUM (garden pea) / References: UniProt: Q9SQL2 |
| #7: Protein | Mass: 8991.474 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) PISUM SATIVUM (garden pea) / References: UniProt: P10793 |
-PHOTOSYSTEM I P700 CHLOROPHYLL A APOPROTEIN ... , 2 types, 2 molecules AB
| #5: Protein | Mass: 84284.516 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) PISUM SATIVUM (garden pea) / References: UniProt: P05310 |
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| #6: Protein | Mass: 82490.961 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) PISUM SATIVUM (garden pea) / References: UniProt: P05311 |
-PHOTOSYSTEM I REACTION CENTER SUBUNIT ... , 9 types, 9 molecules DEFGHIJKL
| #8: Protein | Mass: 23170.641 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) SPINACIA OLERACEA (spinach) / References: UniProt: P12353 |
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| #9: Protein | Mass: 14984.955 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #10: Protein | Mass: 25445.453 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) SPINACIA OLERACEA (spinach) / References: UniProt: P12355 |
| #11: Protein | Mass: 18232.650 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) SPINACIA OLERACEA (spinach) / References: UniProt: P12357 |
| #12: Protein | Mass: 15341.604 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) SPINACIA OLERACEA (spinach) / References: UniProt: P22179 |
| #13: Protein/peptide | Mass: 4474.527 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) PISUM SATIVUM (garden pea) / References: UniProt: P17227 |
| #14: Protein/peptide | Mass: 5079.930 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) SPINACIA OLERACEA (spinach) / References: UniProt: P17230 |
| #15: Protein | Mass: 13742.934 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) ![]() |
| #16: Protein | Mass: 22957.676 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) SPINACIA OLERACEA (spinach) / References: UniProt: Q41385 |
-PHOTOSYSTEM I-N ... , 2 types, 2 molecules NR
| #17: Protein | Mass: 18460.988 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) PHASEOLUS VULGARIS (common bean) / References: UniProt: Q84U30 |
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| #18: Protein | Mass: 4528.573 Da / Num. of mol.: 1 / Source method: isolated from a natural source / Source: (natural) PISUM SATIVUM (garden pea) |
-Sugars , 2 types, 58 molecules 
| #19: Polysaccharide | beta-D-fructofuranose-(2-1)-alpha-D-glucopyranose / sucrose #21: Sugar | ChemComp-LMU / |
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-Non-polymers , 6 types, 198 molecules 








| #20: Chemical | ChemComp-CLA / #22: Chemical | ChemComp-BCR / #23: Chemical | #24: Chemical | #25: Chemical | ChemComp-LMG / | #26: Chemical | ChemComp-UNL / | Num. of mol.: 1 / Source method: obtained synthetically |
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-Details
| Has protein modification | Y |
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-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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Sample preparation
| Crystal | Density Matthews: 2.3 Å3/Da / Density % sol: 44 % / Description: NONE |
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| Crystal grow | pH: 6 Details: 22.5 MM MES BIS-TRIS PH 6 10MM SUCCINIC ACID 6% PEG6000 0.015% DTM |
-Data collection
| Diffraction | Mean temperature: 100 K |
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| Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID23-2 / Wavelength: 0.873 |
| Detector | Type: MARRESEARCH / Detector: CCD / Date: Mar 12, 2009 / Details: MIRRORS |
| Radiation | Monochromator: SI(111) / Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.873 Å / Relative weight: 1 |
| Reflection | Resolution: 3.3→50 Å / Num. obs: 88964 / % possible obs: 99 % / Observed criterion σ(I): 2 / Redundancy: 4.3 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 17.2 |
| Reflection shell | Resolution: 3.3→3.43 Å / Redundancy: 3.7 % / Rmerge(I) obs: 0.4 / Mean I/σ(I) obs: 2.8 / % possible all: 95.2 |
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Processing
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| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: PDB ENTRY 1YO9 Resolution: 3.3→30 Å / Cor.coef. Fo:Fc: 0.771 / Cor.coef. Fo:Fc free: 0.762 / SU B: 0.001 / SU ML: 0 / Cross valid method: THROUGHOUT / Stereochemistry target values: MAXIMUM LIKELIHOOD / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.
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| Solvent computation | Solvent model: NONE | ||||||||||||||||||||
| Displacement parameters | Biso mean: 23.117 Å2
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| Refinement step | Cycle: LAST / Resolution: 3.3→30 Å
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| LS refinement shell | Resolution: 3.3→3.385 Å / Total num. of bins used: 20
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