› 3i2e

X-ray diffraction
2.03Å resolution

Crystal structure of human dimethylarginine dymethylaminohydrolase-1 (DDAH-1)

Released:
DOI: 10.2210/pdb3i2e/pdb
PDB entry 3i2e coloured by chain, front view.
PDB entry 3i2e coloured by chain, side view.
PDB entry 3i2e coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Developing dual and specific inhibitors of dimethylarginine dimethylaminohydrolase-1 and nitric oxide synthase: toward a targeted polypharmacology to control nitric oxide.
Wang Y, Monzingo AF, Hu S, Schaller TH, Robertus JD, Fast W
Biochemistry 48 8624-35 (2009)
PMID: 19663506

Function and Biology Details

Reaction catalysed: 
N(omega),N(omega)-dimethyl-L-arginine + H(2)O = dimethylamine + L-citrulline
Biochemical function:
Biological process:
Cellular component:
Sequence domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-131736 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N(G),N(G)-dimethylarginine dimethylaminohydrolase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 308 amino acids
Theoretical weight: 33.62 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: O94760 (Residues: 1-285; Coverage: 100%)
Gene names: DDAH, DDAH1
Sequence domains: N,N dimethylarginine dimethylhydrolase, eukaryotic
Structure domains: L-arginine/glycine Amidinotransferase; Chain A

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21
Unit cell:
a: 72.995Å b: 47.926Å c: 90.318Å
α: 90° β: 94.16° γ: 90°
R-values:
R R work R free
0.189 0.189 0.225
Expression system: Escherichia coli

Quick links

Citations

7 review citations

The therapeutic potential of targeting endogenous inhibitors of nitric oxide synthesis.
Leiper et al. (2011)
6 more

3 mentions without citation

Developing dual and specific inhibitors of dimethylarginine dimethylaminohydrolase-1 and nitric oxide synthase: toward a targeted polypharmacology to control nitric oxide.
Wang et al. (2009)
2 more