› 1ky4

X-ray diffraction
2.8Å resolution

S-Adenosylhomocysteine hydrolase refined with noncrystallographic restraints

Released:
DOI: 10.2210/pdb1ky4/pdb
PDB 1ky4 coloured by chain and viewed from the front.
PDB 1ky4 coloured by chain and viewed from the side.
PDB 1ky4 coloured by chain and viewed from the top.
Source organism: Rattus norvegicus
Primary publication:
Catalytic mechanism of S-adenosylhomocysteine hydrolase. Site-directed mutagenesis of Asp-130, Lys-185, Asp-189, and Asn-190.
Takata Y, Yamada T, Huang Y, Komoto J, Gomi T, Ogawa H, Fujioka M, Takusagawa F
J Biol Chem 277 22670-6 (2002)
PMID: 11927587

Function and Biology Details

Reaction catalysed: 
S-adenosyl-L-homocysteine + H(2)O = L-homocysteine + adenosine
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenosylhomocysteinase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 431 amino acids
Theoretical weight: 47.47 KDa
Source organism: Rattus norvegicus
Expression system: Escherichia coli
UniProt:
  • Canonical: P10760 (Residues: 2-432; Coverage: 100%)
Gene name: Ahcy
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand NAD 4 x NAD
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 94.76Å b: 134.48Å c: 102.26Å
α: 90° β: 114.35° γ: 90°
R-values:
R R work R free
0.23 0.228 0.278
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Metabolism and regulation of glycerolipids in the yeast Saccharomyces cerevisiae.
Henry et al. (2012)
27 other articles

4 mentions without citation

S-adenosyl-L-homocysteine hydrolase and methylation disorders: yeast as a model system.
Tehlivets et al. (2013)
3 more