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- PDB-5xnf: Crystal structure of the branched-chain polyamine synthase (BpsA)... -
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Open data
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Basic information
Entry | Database: PDB / ID: 5xnf | ||||||
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Title | Crystal structure of the branched-chain polyamine synthase (BpsA) from Thermococcus kodakarensis | ||||||
![]() | N(4)-bis(aminopropyl)spermidine synthase | ||||||
![]() | TRANSFERASE / Polyamine biosynthesis / N(4)-bis(aminopropyl)spermidine synthase | ||||||
Function / homology | ![]() 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 | ![]() ![]() | ||||||
Method | ![]() ![]() ![]() | ||||||
![]() | Mizohata, E. / Tse, K.M. / Fujita, J. / Inoue, T. | ||||||
![]() | ![]() 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: ![]() ![]() |
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Downloads & links
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Download
PDBx/mmCIF format | ![]() | 290.9 KB | Display | ![]() |
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PDB format | ![]() | 236 KB | Display | ![]() |
PDBx/mmJSON format | ![]() | Tree view | ![]() | |
Others | ![]() |
-Validation report
Summary document | ![]() | 473.4 KB | Display | ![]() |
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Full document | ![]() | 486.6 KB | Display | |
Data in XML | ![]() | 28.7 KB | Display | |
Data in CIF | ![]() | 39.9 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 5xncC ![]() 5xnhC ![]() 2qm3S 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: 42445.941 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) ![]() ![]() Strain: ATCC BAA-918 / JCM 12380 / KOD1 / Gene: bpsA, TK1691 / Plasmid: pET28a Details (production host): N-terminal HisTag/thrombin/T7 tag Production host: ![]() ![]() References: UniProt: Q5JIZ3, N4-bis(aminopropyl)spermidine synthase #2: Chemical | ChemComp-FE / | #3: Chemical | #4: Chemical | ChemComp-GOL / | #5: Water | ChemComp-HOH / | |
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-Experimental details
-Experiment
Experiment | Method: ![]() |
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Sample preparation
Crystal | Density Matthews: 2.35 Å3/Da / Density % sol: 47.75 % |
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Crystal grow | Temperature: 293 K / Method: vapor diffusion, sitting drop / pH: 7.2 Details: 100mM NaCl, 100mM lithium sulfate, 100mM ADA (pH6.5), 11.5% (w/v) PEG 4000 |
-Data collection
Diffraction | Mean temperature: 100 K / Ambient temp details: cryogenic temperature |
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Diffraction source | Source: ![]() ![]() ![]() |
Detector | Type: RAYONIX MX300HE / Detector: CCD / Date: May 17, 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: 1.9→50 Å / Num. obs: 60904 / % possible obs: 100 % / Redundancy: 14.6 % / Rsym value: 0.109 / Net I/σ(I): 23.6 |
Reflection shell | Resolution: 1.9→1.97 Å / Redundancy: 14.3 % / Mean I/σ(I) obs: 1.3 / % possible all: 100 |
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Processing
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Refinement | Method to determine structure: ![]() Starting model: 2QM3 Resolution: 1.9→50 Å / Cor.coef. Fo:Fc: 0.972 / Cor.coef. Fo:Fc free: 0.957 / SU B: 12.461 / SU ML: 0.156 / Cross valid method: THROUGHOUT / ESU R: 0.162 / ESU R Free: 0.15 / 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: 42.83 Å2
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Refinement step | Cycle: LAST / Resolution: 1.9→50 Å
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Refine LS restraints |
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