› 4lc5

X-ray diffraction
1.97Å resolution

Structural basis of substrate specificity of CDA superfamily guanine deaminase

Released:
DOI: 10.2210/pdb4lc5/pdb
PDB entry 4lc5 coloured by chain, front view.
PDB entry 4lc5 coloured by chain, side view.
PDB entry 4lc5 coloured by chain, top view.
Source organism: Nitrosomonas europaea ATCC 19718
Primary publication:
Structural basis of the substrate specificity of cytidine deaminase superfamily Guanine deaminase.
Bitra A, Biswas A, Anand R
Biochemistry 52 8106-14 (2013)
PMID: 24083949

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-182725 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CMP/dCMP-type deaminase domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 197 amino acids
Theoretical weight: 20.59 KDa
Source organism: Nitrosomonas europaea ATCC 19718
Expression system: Escherichia coli
UniProt:
  • Canonical: Q82Y41 (Residues: 1-193; Coverage: 100%)
Gene name: NE0047
Sequence domains: Cytidine and deoxycytidylate deaminase zinc-binding region
Structure domains: Cytidine Deaminase, domain 2

Ligands and Environments

3 bound ligands:
Ligand ZN 2 x ZN
Ligand 9MG 1 x 9MG
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM14
Spacegroup: P212121
Unit cell:
a: 38.15Å b: 74.18Å c: 109.78Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.164 0.217
Expression system: Escherichia coli

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Citations

3 citation in other articles

An Ultra-Robust and Crystalline Redeemable Hydrogen-Bonded Organic Framework for Synergistic Chemo-Photodynamic Therapy.
Yin et al. (2018)
2 more

1 mention without citation

Nucleobase deaminases: a potential enzyme system for new therapies.
Gaded et al. (2018)