PDBe 3iar

X-ray diffraction
1.52Å resolution

The crystal structure of human adenosine deaminase

Released:
Source organism: Homo sapiens
Entry authors: Ugochukwu E, Zhang Y, Hapka E, Yue WW, Bray JE, Muniz J, Burgess-Brown N, Chaikuad A, von Delft F, Bountra C, Arrowsmith CH, Weigelt J, Edwards A, Kavanagh KL, Oppermann U, Structural Genomics Consortium (SGC)

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: 367 amino acids
Theoretical weight: 41.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P00813 (Residues: 5-363; Coverage: 99%)
Gene names: ADA, ADA1
Sequence domains: Adenosine/AMP deaminase
Structure domains: Metal-dependent hydrolases

Ligands and Environments


No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E SUPERBRIGHT
Spacegroup: P212121
Unit cell:
a: 61.07Å b: 73.51Å c: 76.66Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.153 0.185
Expression system: Escherichia coli