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TitleMultifunctionality of arginine residues in the active sites of non-canonical d-amino acid transaminases.
Journal, issue, pagesArch. Biochem. Biophys., Vol. 756, Page 110011-110011, Year 2024
Publish dateDec 1, 2023 (structure data deposition date)
AuthorsBakunova, A.K. / Matyuta, I.O. / Minyaev, M.E. / Isaikina, T.Y. / Boyko, K.M. / Popov, V.O. / Bezsudnova, E.Y.
External linksArch. Biochem. Biophys. / PubMed:38649133
MethodsX-ray diffraction
Resolution2 Å
Structure data

PDB-8raf:
Crystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis point mutant R90I (holo form)
Method: X-RAY DIFFRACTION / Resolution: 2 Å

PDB-8rai:
Crystal structure of D-amino acid transaminase from Haliscomenobacter hydrossis point mutant R90I complexed with phenylhydrazine
Method: X-RAY DIFFRACTION / Resolution: 2 Å

Chemicals

ChemComp-PLP:
PYRIDOXAL-5'-PHOSPHATE

ChemComp-HOH:
WATER

ChemComp-ZXN:
[6-methyl-5-oxidanyl-4-[(2-phenylhydrazinyl)methyl]pyridin-3-yl]methyl dihydrogen phosphate

ChemComp-GOL:
GLYCEROL

Source
  • haliscomenobacter hydrossis dsm 1100 (bacteria)
KeywordsTRANSFERASE / DAAT / point mutant / aminotransferase / transaminase / Haliscomenobacter hydrossis / phenylhydrazine / complex

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