› 4pgf

X-ray diffraction
2.59Å resolution

The structure of mono-acetylated SAHH

Released:
DOI: 10.2210/pdb4pgf/pdb
PDB entry 4pgf coloured by chain, front view.
PDB entry 4pgf coloured by chain, side view.
PDB entry 4pgf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Regulation of S-adenosylhomocysteine hydrolase by lysine acetylation.
Wang Y, Kavran JM, Chen Z, Karukurichi KR, Leahy DJ, Cole PA
J Biol Chem 289 31361-72 (2014)
PMID: 25248746

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149993 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenosylhomocysteinase Chains: A, B
Molecule details ›
Chains: A, B
Length: 432 amino acids
Theoretical weight: 47.79 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P23526 (Residues: 1-432; Coverage: 100%)
Gene names: AHCY, SAHH
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand NAD 2 x NAD
Ligand ADN 2 x ADN
1 modified residue:
Ligand ALY 2 x ALY

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: I222
Unit cell:
a: 97.597Å b: 102.74Å c: 175.018Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 0.188 0.248
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Metabolic regulation of histone post-translational modifications.
Fan et al. (2015)
5 more

1 mention without citation

Regulation of S-adenosylhomocysteine hydrolase by lysine acetylation.
Wang et al. (2014)