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-Structure paper
Title | Active site geometry of a novel aminopropyltransferase for biosynthesis of hyperthermophile-specific branched-chain polyamine. |
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Journal, issue, pages | FEBS J., Vol. 284, Page 3684-3701, Year 2017 |
Publish date | May 22, 2017 (structure data deposition date) |
Authors | Hidese, R. / Tse, K.M. / Kimura, S. / Mizohata, E. / Fujita, J. / Horai, Y. / Umezawa, N. / Higuchi, T. / Niitsu, M. / Oshima, T. ...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. |
External links | FEBS J. / PubMed:28881427 |
Methods | X-ray diffraction |
Resolution | 1.84 - 1.95 Å |
Structure data | PDB-5xnc: PDB-5xnf: PDB-5xnh: |
Chemicals | ChemComp-MTA: ChemComp-N4P: ChemComp-GOL: ChemComp-FE: ChemComp-PEG: ChemComp-EDO: ChemComp-HOH: ChemComp-SO4: ChemComp-SPD: |
Source |
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Keywords | TRANSFERASE / Polyamine biosynthesis / spermidine / N4-aminopropylspermidine / Branched polyamines / N(4)-bis(aminopropyl)spermidine synthase |