[English] 日本語
Yorodumi- PDB-5b5n: Crystal structure of the Ba-substituted LH1-RC complex from Tch. ... -
+
Open data
-
Basic information
| Entry | Database: PDB / ID: 5b5n | ||||||
|---|---|---|---|---|---|---|---|
| Title | Crystal structure of the Ba-substituted LH1-RC complex from Tch. tepidum | ||||||
Components |
| ||||||
Keywords | PHOTOSYNTHESIS / Bacterial photosynthesis / Light-harvesting complex | ||||||
| Function / homology | Function and homology informationorganelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / : / photosynthesis, light reaction / photosynthesis / endomembrane system / electron transfer activity ...organelle inner membrane / plasma membrane-derived chromatophore membrane / plasma membrane light-harvesting complex / bacteriochlorophyll binding / photosynthetic electron transport in photosystem II / : / photosynthesis, light reaction / photosynthesis / endomembrane system / electron transfer activity / iron ion binding / heme binding / metal ion binding / membrane / plasma membrane Similarity search - Function | ||||||
| Biological species | Thermochromatium tepidum (bacteria) | ||||||
| Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 3.3 Å | ||||||
Authors | Wang-Otomo, Z.-Y. / Yu, L.-J. | ||||||
Citation | Journal: Biochemistry / Year: 2016Title: Structural Basis for the Unusual Qy Red-Shift and Enhanced Thermostability of the LH1 Complex from Thermochromatium tepidum. Authors: Yu, L.J. / Kawakami, T. / Kimura, Y. / Wang-Otomo, Z.Y. | ||||||
| History |
|
-
Structure visualization
| Structure viewer | Molecule: Molmil Jmol/JSmol |
|---|
-
Downloads & links
-
Download
| PDBx/mmCIF format | 5b5n.cif.gz | 2.6 MB | Display | PDBx/mmCIF format |
|---|---|---|---|---|
| PDB format | pdb5b5n.ent.gz | Display | PDB format | |
| PDBx/mmJSON format | 5b5n.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 5b5n_validation.pdf.gz | 23.5 MB | Display | wwPDB validaton report |
|---|---|---|---|---|
| Full document | 5b5n_full_validation.pdf.gz | 24.1 MB | Display | |
| Data in XML | 5b5n_validation.xml.gz | 291.4 KB | Display | |
| Data in CIF | 5b5n_validation.cif.gz | 333.1 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/b5/5b5n ftp://data.pdbj.org/pub/pdb/validation_reports/b5/5b5n | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 5b5mC ![]() 3wmmS C: citing same article ( S: Starting model for refinement |
|---|---|
| Similar structure data |
-
Links
-
Assembly
| Deposited unit | ![]()
| ||||||||
|---|---|---|---|---|---|---|---|---|---|
| 1 | ![]()
| ||||||||
| 2 | ![]()
| ||||||||
| Unit cell |
|
-
Components
-Photosynthetic reaction center ... , 4 types, 8 molecules CoLxMyHt
| #1: Protein | Mass: 36630.484 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 1-333 / Source method: isolated from a natural source / Source: (natural) Thermochromatium tepidum (bacteria) / References: UniProt: D2Z0P5#2: Protein | Mass: 31520.771 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermochromatium tepidum (bacteria) / References: UniProt: D2Z0P3#3: Protein | Mass: 35975.992 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 1-319 / Source method: isolated from a natural source / Source: (natural) Thermochromatium tepidum (bacteria) / References: UniProt: A8ASG6#4: Protein | Mass: 28213.305 Da / Num. of mol.: 2 / Source method: isolated from a natural source / Source: (natural) Thermochromatium tepidum (bacteria) / References: UniProt: D2Z0P9 |
|---|
-Protein / Protein/peptide , 2 types, 64 molecules ADFIKOQSUWY13579mpruwAAACAEAGAIAKdfh...
| #5: Protein | Mass: 7034.442 Da / Num. of mol.: 32 / Source method: isolated from a natural source / Source: (natural) Thermochromatium tepidum (bacteria) / References: UniProt: D2Z0P2#6: Protein/peptide | Mass: 5534.452 Da / Num. of mol.: 32 / Source method: isolated from a natural source / Source: (natural) Thermochromatium tepidum (bacteria) / References: UniProt: D2Z0P1 |
|---|
-Non-polymers , 12 types, 190 molecules 






















| #7: Chemical | ChemComp-HEM / #8: Chemical | ChemComp-BA / #9: Chemical | ChemComp-BCL / #10: Chemical | ChemComp-BPH / #11: Chemical | #12: Chemical | ChemComp-PEF / #13: Chemical | #14: Chemical | #15: Chemical | ChemComp-CRT / #16: Chemical | ChemComp-PO4 / #17: Chemical | #18: Water | ChemComp-HOH / | |
|---|
-Experimental details
-Experiment
| Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
|---|
-
Sample preparation
| Crystal | Density Matthews: 3.14 Å3/Da / Density % sol: 60.78 % |
|---|---|
| Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / Details: PEG 3000, barium chloride, decylphosphocholine |
-Data collection
| Diffraction | Mean temperature: 100 K |
|---|---|
| Diffraction source | Source: SYNCHROTRON / Site: Photon Factory / Beamline: BL-17A / Wavelength: 0.98 Å |
| Detector | Type: ADSC QUANTUM 270 / Detector: CCD / Date: Feb 16, 2013 |
| Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
| Radiation wavelength | Wavelength: 0.98 Å / Relative weight: 1 |
| Reflection | Resolution: 3.3→49.9 Å / Num. obs: 133051 / % possible obs: 93 % / Redundancy: 22.8 % / Net I/σ(I): 8.6 |
| Reflection shell | Resolution: 3.3→3.36 Å |
-
Processing
| Software |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Refinement | Method to determine structure: MOLECULAR REPLACEMENTStarting model: 3WMM Resolution: 3.3→49.9 Å / SU ML: 0.55 / Cross valid method: FREE R-VALUE / σ(F): 1.38 / Phase error: 35.57 / Stereochemistry target values: ML
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Solvent computation | Shrinkage radii: 0.9 Å / VDW probe radii: 1.11 Å / Solvent model: FLAT BULK SOLVENT MODEL | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement step | Cycle: LAST / Resolution: 3.3→49.9 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refine LS restraints |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| LS refinement shell |
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement TLS params. | Method: refined / Origin x: 24.59 Å / Origin y: -15.8433 Å / Origin z: 49.1244 Å
| |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| Refinement TLS group | Selection details: all |
Movie
Controller
About Yorodumi



Thermochromatium tepidum (bacteria)
X-RAY DIFFRACTION
Citation









PDBj






