› 4hrq

X-ray diffraction
1.9Å resolution

Identification of Function and Mechanistic Insights of Guanine Deaminase from Nitrosomonas europaea: Role of the C-terminal Loop in Catalysis

Released:
DOI: 10.2210/pdb4hrq/pdb
PDB entry 4hrq coloured by chain, front view.
PDB entry 4hrq coloured by chain, side view.
PDB entry 4hrq coloured by chain, top view.
Source organism: Nitrosomonas europaea ATCC 19718
Primary publication:
Identification of function and mechanistic insights of guanine deaminase from Nitrosomonas europaea: role of the C-terminal loop in catalysis.
Bitra A, Hussain B, Tanwar AS, Anand R
Biochemistry 52 3512-22 (2013)
PMID: 23557066

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
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

2 bound ligands:
Ligand AZG 2 x AZG
Ligand ZN 2 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E DW
Spacegroup: P212121
Unit cell:
a: 38.254Å b: 74.123Å c: 110.189Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.22 0.22 0.246
Expression system: Escherichia coli

Quick links

Citations

2 citation in other articles

Solution structure of the nucleotide hydrolase BlsM: Implication of its substrate specificity.
Kang et al. (2020)
1 more

1 mention without citation

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