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Yorodumi- PDB-5xww: Substrate-bound Structure of G355T/Q364H mutant of a Ketoreductas... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5xww | ||||||||||||
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Title | Substrate-bound Structure of G355T/Q364H mutant of a Ketoreductase from amphotericin Polyketide Synthases | ||||||||||||
Components | AmphB | ||||||||||||
Keywords | OXIDOREDUCTASE / modular polyketide synthease / ketoreductase / mutant | ||||||||||||
Function / homology | Function and homology information macrolide biosynthetic process / phosphopantetheine binding / 3-oxoacyl-[acyl-carrier-protein] synthase activity / fatty acid biosynthetic process / nucleotide binding / identical protein binding Similarity search - Function | ||||||||||||
Biological species | Streptomyces nodosus (bacteria) | ||||||||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / MOLECULAR REPLACEMENT / Resolution: 1.96 Å | ||||||||||||
Authors | Liu, C. / Zheng, J. | ||||||||||||
Funding support | China, 3items
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Citation | Journal: J. Struct. Biol. / Year: 2018 Title: Substrate-bound structures of a ketoreductase from amphotericin modular polyketide synthase. Authors: Liu, C. / Yuan, M. / Xu, X. / Wang, L. / Keatinge-Clay, A.T. / Deng, Z. / Lin, S. / Zheng, J. | ||||||||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5xww.cif.gz | 348 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5xww.ent.gz | 280.5 KB | Display | PDB format |
PDBx/mmJSON format | 5xww.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xw/5xww ftp://data.pdbj.org/pub/pdb/validation_reports/xw/5xww | HTTPS FTP |
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-Related structure data
Related structure data | 5xwvC 3mjeS 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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1 |
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Unit cell |
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Noncrystallographic symmetry (NCS) | NCS domain:
NCS domain segments: Component-ID: 0 / Ens-ID: 1 / Beg auth comp-ID: GLY / Beg label comp-ID: GLY / End auth comp-ID: SER / End label comp-ID: SER / Refine code: 0 / Auth seq-ID: -3 - 473 / Label seq-ID: 18 - 494
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-Components
#1: Protein | Mass: 51478.766 Da / Num. of mol.: 2 / Fragment: UNP RESIDUES 2529-3003 / Mutation: G355T, Q364H Source method: isolated from a genetically manipulated source Source: (gene. exp.) Streptomyces nodosus (bacteria) / Gene: amphB / Production host: Escherichia coli (E. coli) / References: UniProt: Q93NW7 #2: Chemical | #3: Chemical | #4: Water | ChemComp-HOH / | |
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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: 2.36 Å3/Da / Density % sol: 48 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion / pH: 7.5 / Details: 3.4 M ammonium sulfate, 0.1 M HEPES, pH 7.5 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SSRF / Beamline: BL18U1 / Wavelength: 0.9778 Å |
Detector | Type: DECTRIS PILATUS3 6M / Detector: PIXEL / Date: Dec 21, 2016 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9778 Å / Relative weight: 1 |
Reflection | Resolution: 1.96→62.48 Å / Num. obs: 63286 / % possible obs: 94.6 % / Redundancy: 1.8 % / Rmerge(I) obs: 0.1 / Net I/σ(I): 8.6 |
Reflection shell | Resolution: 1.96→1.99 Å / Redundancy: 1.6 % / Rmerge(I) obs: 0.368 / Mean I/σ(I) obs: 2 / Num. unique obs: 3033 / % possible all: 90.6 |
-Processing
Software |
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Refinement | Method to determine structure: MOLECULAR REPLACEMENT Starting model: 3MJE Resolution: 1.96→50 Å / Cor.coef. Fo:Fc: 0.957 / Cor.coef. Fo:Fc free: 0.939 / SU B: 8.716 / SU ML: 0.116 / Cross valid method: THROUGHOUT / ESU R: 0.176 / ESU R Free: 0.153 / Stereochemistry target values: MAXIMUM LIKELIHOOD / 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 / Solvent model: MASK | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Displacement parameters | Biso mean: 31.437 Å2
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Refinement step | Cycle: 1 / Resolution: 1.96→50 Å
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Refine LS restraints |
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