+Open data
-Basic information
Entry | Database: PDB / ID: 1uw9 | ||||||
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Title | L290F-A222T chlamydomonas Rubisco mutant | ||||||
Components | (RIBULOSE BISPHOSPHATE CARBOXYLASE ...) x 2 | ||||||
Keywords | LYASE / RUBISCO / PHOTOSYNTHESIS / PHOTORESPIRATION / OXIDOREDUCTASE / MONOOXYGENASE / CARBON DIOXIDE FIXATION | ||||||
Function / homology | Function and homology information photorespiration / ribulose-bisphosphate carboxylase / ribulose-bisphosphate carboxylase activity / reductive pentose-phosphate cycle / monooxygenase activity / chloroplast / magnesium ion binding Similarity search - Function | ||||||
Biological species | CHLAMYDOMONAS REINHARDTII (plant) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 2.05 Å | ||||||
Authors | Karkehabadi, S. / Taylor, T.C. / Spreitzer, R.J. / Andersson, I. | ||||||
Citation | Journal: Biochemistry / Year: 2005 Title: Altered Intersubunit Interactions in Crystal Structures of Catalytically Compromised Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Authors: Karkehabadi, S. / Taylor, T.C. / Spreitzer, R.J. / Andersson, I. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 1uw9.cif.gz | 990.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb1uw9.ent.gz | 825.4 KB | Display | PDB format |
PDBx/mmJSON format | 1uw9.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 1uw9_validation.pdf.gz | 2.8 MB | Display | wwPDB validaton report |
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Full document | 1uw9_full_validation.pdf.gz | 2.9 MB | Display | |
Data in XML | 1uw9_validation.xml.gz | 198 KB | Display | |
Data in CIF | 1uw9_validation.cif.gz | 279.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/uw/1uw9 ftp://data.pdbj.org/pub/pdb/validation_reports/uw/1uw9 | HTTPS FTP |
-Related structure data
Related structure data | 1uwaC 1gk8S S: Starting model for refinement C: citing same article (ref.) |
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Similar structure data |
-Links
-Assembly
Deposited unit |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS oper:
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Details | FOR THE HETERO-ASSEMBLY DESCRIBED BY REMARK 350 |
-Components
-RIBULOSE BISPHOSPHATE CARBOXYLASE ... , 2 types, 16 molecules ABEHKORVCFIJMPTW
#1: Protein | Mass: 52760.883 Da / Num. of mol.: 8 / Mutation: YES / Source method: isolated from a natural source / Source: (natural) CHLAMYDOMONAS REINHARDTII (plant) References: UniProt: P00877, ribulose-bisphosphate carboxylase #2: Protein | Mass: 16294.788 Da / Num. of mol.: 8 / Source method: isolated from a natural source / Source: (natural) CHLAMYDOMONAS REINHARDTII (plant) References: UniProt: P00873, ribulose-bisphosphate carboxylase |
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-Sugars , 1 types, 8 molecules
#4: Sugar | ChemComp-CAP / |
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-Non-polymers , 3 types, 2882 molecules
#3: Chemical | ChemComp-MG / #5: Chemical | ChemComp-EDO / #6: Water | ChemComp-HOH / | |
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-Details
Compound details | ENGINEERED MUTATION ALA 222 THR AND LEU 290 PHE IN CHAINS A, B, E, H, K, O, R AND V. RUBISCO ...ENGINEERED |
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Sequence details | RESIDUE 46 IN THE LARGE SUBUNITS (CHAIN A B E H K O R V) HAS BEEN IDENTIFIED |
-Experimental details
-Experiment
Experiment | Method: X-RAY DIFFRACTION / Number of used crystals: 1 |
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-Sample preparation
Crystal | Density Matthews: 2.11 Å3/Da / Density % sol: 41.81 % |
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Crystal grow | Temperature: 291 K / pH: 7.5 Details: 0 MM HEPES PH 7.5, 8-12% PEG 4 50 MM NAHCO3, 5 MM MGCL2, 50 UM 2-CABP, 18 DEG C, 10-15 MG PROTEIN |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: ESRF / Beamline: ID14-1 / Wavelength: 0.934 |
Detector | Date: Feb 23, 2001 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.934 Å / Relative weight: 1 |
Reflection | Resolution: 2.05→20 Å / Num. obs: 295370 / % possible obs: 88.9 % / Redundancy: 6.3 % / Rmerge(I) obs: 0.15 / Net I/σ(I): 8.9 |
Reflection shell | Resolution: 2.05→2.09 Å / Rmerge(I) obs: 0.49 / Mean I/σ(I) obs: 1.8 / % possible all: 83.5 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: PDB ENTRY 1GK8 Resolution: 2.05→20 Å / SU B: 4.513 / SU ML: 0.118 / Cross valid method: THROUGHOUT / ESU R: 0.29 / ESU R Free: 0.184
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Displacement parameters | Biso mean: 18.147 Å2
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Refinement step | Cycle: LAST / Resolution: 2.05→20 Å
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