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Yorodumi- PDB-5xnh: Crystal structure of the branched-chain polyamine synthase (BpsA)... -
+Open data
-Basic information
Entry | Database: PDB / ID: 5xnh | ||||||
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Title | Crystal structure of the branched-chain polyamine synthase (BpsA) in complex with spermidine | ||||||
Components | N(4)-bis(aminopropyl)spermidine synthase | ||||||
Keywords | TRANSFERASE / Polyamine biosynthesis / N(4)-bis(aminopropyl)spermidine synthase | ||||||
Function / homology | Function and homology information N4-bis(aminopropyl)spermidine synthase / rRNA (adenine-N6-)-methyltransferase activity / polyamine biosynthetic process / transferase activity, transferring alkyl or aryl (other than methyl) groups / transferase activity / cytoplasm Similarity search - Function | ||||||
Biological species | Thermococcus kodakarensis (archaea) | ||||||
Method | X-RAY DIFFRACTION / SYNCHROTRON / Resolution: 1.95 Å | ||||||
Authors | Mizohata, E. / Tse, K.M. / Fujita, J. / Inoue, T. | ||||||
Citation | Journal: FEBS J. / Year: 2017 Title: Active site geometry of a novel aminopropyltransferase for biosynthesis of hyperthermophile-specific branched-chain polyamine. Authors: Hidese, R. / Tse, K.M. / Kimura, S. / Mizohata, E. / Fujita, J. / Horai, Y. / Umezawa, N. / Higuchi, T. / Niitsu, M. / Oshima, T. / Imanaka, T. / Inoue, T. / Fujiwara, S. | ||||||
History |
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-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
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-Downloads & links
-Download
PDBx/mmCIF format | 5xnh.cif.gz | 152.7 KB | Display | PDBx/mmCIF format |
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PDB format | pdb5xnh.ent.gz | 117.9 KB | Display | PDB format |
PDBx/mmJSON format | 5xnh.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Summary document | 5xnh_validation.pdf.gz | 456 KB | Display | wwPDB validaton report |
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Full document | 5xnh_full_validation.pdf.gz | 467.7 KB | Display | |
Data in XML | 5xnh_validation.xml.gz | 27.7 KB | Display | |
Data in CIF | 5xnh_validation.cif.gz | 38.5 KB | Display | |
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/xn/5xnh ftp://data.pdbj.org/pub/pdb/validation_reports/xn/5xnh | HTTPS FTP |
-Related structure data
-Links
-Assembly
Deposited unit |
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1 |
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Unit cell |
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-Components
#1: Protein | Mass: 42445.941 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (archaea) Strain: ATCC BAA-918 / JCM 12380 / KOD1 / Gene: bpsA, TK1691 / Plasmid: pET28a Details (production host): N-terminal HisTag/thrombin digestion site Production host: Escherichia coli (E. coli) / Strain (production host): BL-21CodonPlus(DE3)RIL References: UniProt: Q5JIZ3, N4-bis(aminopropyl)spermidine synthase #2: Chemical | ChemComp-FE / | #3: Chemical | #4: Water | ChemComp-HOH / | Sequence details | In chain A, residue numbers 344, 345 are simply skipped. In chain H, residue numbers 345-347 are ...In chain A, residue numbers 344, 345 are simply skipped. In chain H, residue numbers 345-347 are simply skipped. | |
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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: 1.95 Å3/Da / Density % sol: 36.86 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 8.5 Details: 0.1M Sodium chloride, 0.1M Tris pH 8.5, 12 % w/v PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K |
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Diffraction source | Source: SYNCHROTRON / Site: SPring-8 / Beamline: BL44XU / Wavelength: 0.9 Å |
Detector | Type: RAYONIX MX300HE / Detector: CCD / Date: Dec 13, 2014 |
Radiation | Protocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M / Scattering type: x-ray |
Radiation wavelength | Wavelength: 0.9 Å / Relative weight: 1 |
Reflection | Resolution: 1.95→50.01 Å / Num. obs: 47518 / % possible obs: 99.9 % / Redundancy: 5.6 % / Net I/σ(I): 12.4 |
-Processing
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Refinement | Resolution: 1.95→50.01 Å / Cor.coef. Fo:Fc: 0.953 / Cor.coef. Fo:Fc free: 0.93 / SU B: 4.439 / SU ML: 0.126 / Cross valid method: THROUGHOUT / ESU R: 0.215 / ESU R Free: 0.181 / 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: 25.426 Å2
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Refinement step | Cycle: 1 / Resolution: 1.95→50.01 Å
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Refine LS restraints |
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