› 3lgd

X-ray diffraction
2Å resolution

Crystal structure of human adenosine deaminase growth factor, adenosine deaminase type 2 (ADA2)

Released:
DOI: 10.2210/pdb3lgd/pdb
PDB entry 3lgd coloured by chain, front view.
PDB entry 3lgd coloured by chain, side view.
PDB entry 3lgd coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural basis for the growth factor activity of human adenosine deaminase ADA2.
Zavialov AV, Yu X, Spillmann D, Lauvau G, Zavialov AV
J Biol Chem 285 12367-77 (2010)
PMID: 20147294

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:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192759 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenosine deaminase 2 Chains: A, B
Molecule details ›
Chains: A, B
Length: 508 amino acids
Theoretical weight: 59.05 KDa
Source organism: Homo sapiens
Expression system: Drosophila
UniProt:
  • Canonical: Q9NZK5 (Residues: 29-511; Coverage: 100%)
Gene names: ADA2, ADGF, CECR1, IDGFL
Sequence domains:
Structure domains: Metal-dependent hydrolases

Ligands and Environments

4 bound ligands:
Ligand NAG 6 x NAG
Ligand ZN 2 x ZN
Ligand EDO 2 x EDO
Ligand UNX 2 x UNX
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P1
Unit cell:
a: 63.212Å b: 73.099Å c: 80.662Å
α: 113.38° β: 94.18° γ: 92.16°
R-values:
R R work R free
0.187 0.185 0.234
Expression system: Drosophila

Quick links

Citations

23 review citations

Enzymes involved in metabolism of extracellular nucleotides and nucleosides: functional implications and measurement of activities.
Yegutkin GG. (2014)
22 more

6 mentions without citation

Structural basis for the growth factor activity of human adenosine deaminase ADA2.
Zavialov et al. (2010)
5 more