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- PDB-5msw: Structure of the A-PCP didomain of carboxylic acid reductase (CAR... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5msw | ||||||
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Title | Structure of the A-PCP didomain of carboxylic acid reductase (CAR) from Segniliparus rugosus in complex with AMP | ||||||
![]() | Thioester reductase domain-containing protein | ||||||
![]() | OXIDOREDUCTASE / adenylation domain / carboxylic acid reductase | ||||||
Function / homology | ![]() long-chain fatty acid-CoA ligase activity / : / oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor / Oxidoreductases; Acting on the aldehyde or oxo group of donors; With NAD+ or NADP+ as acceptor / phosphopantetheine binding / NADP binding / ATP binding / membrane Similarity search - Function | ||||||
Biological species | ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Gahloth, D. / Leys, D. | ||||||
![]() | ![]() Title: Structures of carboxylic acid reductase reveal domain dynamics underlying catalysis. Authors: Gahloth, D. / Dunstan, M.S. / Quaglia, D. / Klumbys, E. / Lockhart-Cairns, M.P. / Hill, A.M. / Derrington, S.R. / Scrutton, N.S. / Turner, N.J. / Leys, D. | ||||||
History |
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Structure visualization
Structure viewer | Molecule: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 158.3 KB | Display | ![]() |
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PDB format | ![]() | 117.4 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 751 KB | Display | ![]() |
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Full document | ![]() | 756.5 KB | Display | |
Data in XML | ![]() | 25.6 KB | Display | |
Data in CIF | ![]() | 35.7 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5mscC ![]() 5msdC ![]() 5msoC ![]() 5mspC ![]() 5msrC ![]() 5mssC ![]() 5mstC ![]() 5msuC ![]() 5msvC ![]() 5msqS S: Starting model for refinement 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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Unit cell |
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Components
#1: Protein | Mass: 128368.164 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() Gene: HMPREF9336_01297 / Production host: ![]() ![]() |
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#2: Chemical | ChemComp-AMP / |
#3: Water | ChemComp-HOH / |
-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal grow | Temperature: 277 K / Method: vapor diffusion, sitting drop Details: A-PCP crystals were obtained in 0.2 M sodium fluoride, 0.1 M Bis-Tris Propane pH 6.5 and 20% PEG3350. |
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-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: DECTRIS PILATUS 6M-F / Detector: PIXEL / Date: Jul 20, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9763 Å / Relative weight: 1 |
Reflection | Resolution: 2.33→95.08 Å / Num. obs: 34371 / % possible obs: 99 % / Redundancy: 2.8 % / CC1/2: 1 / Rmerge(I) obs: 0.09 / Net I/σ(I): 10.9 |
Reflection shell | Resolution: 2.33→2.41 Å / CC1/2: 0.5 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 5MSQ Resolution: 2.33→95.08 Å / Cor.coef. Fo:Fc: 0.956 / Cor.coef. Fo:Fc free: 0.929 / SU B: 8.891 / SU ML: 0.199 / Cross valid method: THROUGHOUT / ESU R: 0.332 / ESU R Free: 0.238 / Details: HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS
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Solvent computation | Ion probe radii: 0.8 Å / Shrinkage radii: 0.8 Å / VDW probe radii: 1.2 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 47.076 Å2
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Refinement step | Cycle: 1 / Resolution: 2.33→95.08 Å
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Refine LS restraints |
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