› 1fkw

X-ray diffraction
2.4Å resolution

MURINE ADENOSINE DEAMINASE (D295E)

Released:
DOI: 10.2210/pdb1fkw/pdb
PDB entry 1fkw coloured by chain, front view.
PDB entry 1fkw coloured by chain, side view.
PDB entry 1fkw coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Probing the functional role of two conserved active site aspartates in mouse adenosine deaminase.
Sideraki V, Mohamedali KA, Wilson DK, Chang Z, Kellems RE, Quiocho FA, Rudolph FB
Biochemistry 35 7862-72 (1996)
PMID: 8672487

Function and Biology Details

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

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: 349 amino acids
Theoretical weight: 39.73 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 1 x ZN
Ligand PUR 1 x PUR
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2
Unit cell:
a: 102.84Å b: 94.18Å c: 73.24Å
α: 90° β: 127.37° γ: 90°
R-values:
R R work R free
0.176 0.176 not available
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Adenosine deaminase: functional implications and different classes of inhibitors.
Cristalli et al. (2001)
1 more