› 1xwf

X-ray diffraction
2.8Å resolution

K185N mutated S-adenosylhomocysteine hydrolase

Released:
DOI: 10.2210/pdb1xwf/pdb
PDB entry 1xwf coloured by chain, front view.
PDB entry 1xwf coloured by chain, side view.
PDB entry 1xwf coloured by chain, top view.
Source organism: Rattus norvegicus
Primary publication:
Catalytic mechanism of S-adenosylhomocysteine hydrolase: roles of His 54, Asp130, Glu155, Lys185, and Aspl89.
Yamada T, Takata Y, Komoto J, Gomi T, Ogawa H, Fujioka M, Takusagawa F
Int J Biochem Cell Biol 37 2417-35 (2005)
PMID: 16061414

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145446 (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: 47.45 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

2 bound ligands:
Ligand NAD 4 x NAD
Ligand ADN 4 x ADN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P21
Unit cell:
a: 90.34Å b: 109.37Å c: 104.07Å
α: 90° β: 115.5° γ: 90°
R-values:
R R work R free
0.226 0.225 0.286
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Plant homocysteine, a methionine precursor and plant's hallmark of metabolic disorders.
Sobieszczuk-Nowicka et al. (2022)
18 other articles

2 mentions without citation

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