PDBe 3t1g

X-ray diffraction
2.35Å resolution

Engineering of organophosphate hydrolase by computational design and directed evolution

Released:

Function and Biology Details

Reaction catalysed:
Adenosine + H(2)O = inosine + NH(3)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenosine deaminase Chain: A
Molecule details ›
Chain: A
Length: 353 amino acids
Theoretical weight: 40.18 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P03958 (Residues: 4-352; Coverage: 99%)
Gene name: Ada
Sequence domains: Adenosine/AMP deaminase
Structure domains: Metal-dependent hydrolases

Ligands and Environments

2 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Unit cell:
a: 47.391Å b: 77.592Å c: 94.972Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.189 0.25
Expression system: Escherichia coli BL21(DE3)