› 3t1g

X-ray diffraction
2.35Å resolution

Engineering of organophosphate hydrolase by computational design and directed evolution

Released:
DOI: 10.2210/pdb3t1g/pdb
PDB entry 3t1g coloured by chain, front view.
PDB entry 3t1g coloured by chain, side view.
PDB entry 3t1g coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Computational redesign of a mononuclear zinc metalloenzyme for organophosphate hydrolysis.
Khare SD, Kipnis Y, Greisen P, Takeuchi R, Ashani Y, Goldsmith M, Song Y, Gallaher JL, Silman I, Leader H, Sussman JL, Stoddard BL, Tawfik DS, Baker D
Nat Chem Biol 8 294-300 (2012)
PMID: 22306579

Function and Biology Details

Reaction catalysed: 
2'-deoxyadenosine + H(2)O = 2'-deoxyinosine + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-137300 (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 deaminase
Structure domains: Metal-dependent hydrolases

Ligands and Environments

2 bound ligands:
Ligand ZN 4 x ZN
Ligand CA 1 x CA
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)

Quick links

Citations

40 review citations

Computational enzyme design.
Kiss et al. (2013)
39 more

5 mentions without citation

Protein design: toward functional metalloenzymes.
Yu et al. (2014)
4 more