› 3mvi

X-ray diffraction
1.6Å resolution

Crystal structure of holo mADA at 1.6 A resolution

Released:
DOI: 10.2210/pdb3mvi/pdb
PDB entry 3mvi coloured by chain, front view.
PDB entry 3mvi coloured by chain, side view.
PDB entry 3mvi coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
The role of Zn2+ on the structure and stability of murine adenosine deaminase.
Niu W, Shu Q, Chen Z, Mathews S, Di Cera E, Frieden C
J Phys Chem B 114 16156-65 (2010)
PMID: 20815357

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 Chains: A, B
Molecule details ›
Chains: A, B
Length: 349 amino acids
Theoretical weight: 39.72 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
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 2 x ZN
Ligand GOL 2 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-C
Spacegroup: P21
Unit cell:
a: 46.67Å b: 93.804Å c: 88.048Å
α: 90° β: 105.27° γ: 90°
R-values:
R R work R free
0.17 0.168 0.205
Expression system: Escherichia coli

Quick links

Citations

3 review citations

19F NMR: a valuable tool for studying biological events.
Chen et al. (2013)
2 more

6 mentions without citation

Hydrogen-Deuterium Exchange within Adenosine Deaminase, a TIM Barrel Hydrolase, Identifies Networks for Thermal Activation of Catalysis.
Gao et al. (2020)
5 more