› 1li4

X-ray diffraction
2.01Å resolution

Human S-adenosylhomocysteine hydrolase complexed with neplanocin

Released:
DOI: 10.2210/pdb1li4/pdb
PDB entry 1li4 coloured by chain, front view.
PDB entry 1li4 coloured by chain, side view.
PDB entry 1li4 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Catalytic strategy of S-adenosyl-L-homocysteine hydrolase: transition-state stabilization and the avoidance of abortive reactions.
Yang X, Hu Y, Yin DH, Turner MA, Wang M, Borchardt RT, Howell PL, Kuczera K, Schowen RL
Biochemistry 42 1900-9 (2003)
PMID: 12590576

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-149993 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenosylhomocysteinase Chain: A
Molecule details ›
Chain: A
Length: 432 amino acids
Theoretical weight: 47.77 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

3 bound ligands:
Ligand NAD 1 x NAD
Ligand NOC 1 x NOC
Ligand IPA 2 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X8C
Spacegroup: F222
Unit cell:
a: 92.83Å b: 135.67Å c: 171.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.197 0.197 0.236
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Trans-methylation reactions in plants: focus on the activated methyl cycle.
Rahikainen et al. (2018)
3 more

22 mentions without citation

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