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Structure paper

TitleRegulation of s-adenosylhomocysteine hydrolase by lysine acetylation.
Journal, issue, pagesJ. Biol. Chem., Vol. 289, Page 31361-31372, Year 2014
Publish dateApr 29, 2014 (structure data deposition date)
AuthorsWang, Y. / Kavran, J.M. / Chen, Z. / Karukurichi, K.R. / Leahy, D.J. / Cole, P.A.
External linksJ. Biol. Chem. / PubMed:25248746
MethodsX-ray diffraction
Resolution2.3 - 2.59 Å
Structure data

PDB-4pfj:
The structure of bi-acetylated SAHH
Method: X-RAY DIFFRACTION / Resolution: 2.3 Å

PDB-4pgf:
The structure of mono-acetylated SAHH
Method: X-RAY DIFFRACTION / Resolution: 2.59 Å

Chemicals

ChemComp-NAD:
NICOTINAMIDE-ADENINE-DINUCLEOTIDE / NAD*YM

ChemComp-ADN:
ADENOSINE

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsHYDROLASE / acetylation sahh hydrolase semi-synthetic / hydrolyase acetylation SAHH semi-synthetic

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