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Structure paper

TitleStructural Insights Into the Histidine Trimethylation Activity of Egtd from Mycobacterium Smegmatis.
Journal, issue, pagesBiochem. Biophys. Res. Commun., Vol. 452, Page 1098-, Year 2014
Publish dateAug 29, 2014 (structure data deposition date)
AuthorsJeong, J.H. / Cha, H.J. / Ha, S.C. / Rojviriya, C. / Kim, Y.G.
External linksBiochem. Biophys. Res. Commun. / PubMed:25251321
MethodsX-ray diffraction
Resolution1.997 - 2.306 Å
Structure data

PDB-4uy5:
Crystal structure of Histidine-specific methyltransferase EgtD from Mycobacterium smegmatis
Method: X-RAY DIFFRACTION / Resolution: 1.997 Å

PDB-4uy6:
Crystal structure of Histidine and SAH bound Histidine-specific methyltransferase EgtD from Mycobacterium smegmatis
Method: X-RAY DIFFRACTION / Resolution: 2.04 Å

PDB-4uy7:
Crystal structure of Histidine bound Histidine-specific methyltransferase EgtD from Mycobacterium smegmatis
Method: X-RAY DIFFRACTION / Resolution: 2.306 Å

Chemicals

ChemComp-IMD:
IMIDAZOLE

ChemComp-ACT:
ACETATE ION

ChemComp-HOH:
WATER

ChemComp-HIS:
HISTIDINE

ChemComp-SAH:
S-ADENOSYL-L-HOMOCYSTEINE

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

Source
  • mycobacterium smegmatis (bacteria)
KeywordsTRANSFERASE / S-ADENOSYL-L-METHIONINE / ANTIOXIDANT / MYCOBACTERIUM SMEGMATIS

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