› 7c0j

X-ray diffraction
2.75Å resolution

Crystal structure of chimeric mutant of GH5 in complex with Z-DNA

Released:
DOI: 10.2210/pdb7c0j/pdb
PDB entry 7c0j coloured by chain, front view.
PDB entry 7c0j coloured by chain, side view.
PDB entry 7c0j coloured by chain, top view.
Source organisms:
Primary publication:
Dual conformational recognition by Z-DNA binding protein is important for the B-Z transition process.
Park C, Zheng X, Park CY, Kim J, Lee SK, Won H, Choi J, Kim YG, Choi HJ
Nucleic Acids Res 48 12957-12971 (2020)
PMID: 33245772

Function and Biology Details

Reaction catalysed: 
Adenine in double-stranded RNA + H(2)O = hypoxanthine in double-stranded RNA + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-121137 (preferred)
Entry contents:
1 distinct polypeptide molecule
1 distinct DNA molecule
Macromolecules (2 distinct):
Double-stranded RNA-specific adenosine deaminase; Histone H5 Chains: A, B
Molecule details ›
Chains: A, B
Length: 76 amino acids
Theoretical weight: 8.11 KDa
Source organisms: Expression system: Escherichia coli
UniProt:
  • Canonical: P02259 (Residues: 25-64, 77-88, 92-93, 96-98; Coverage: 30%)
  • Canonical: P55265 (Residues: 169-179, 192-192, 195-196; Coverage: 1%)
Gene names: ADAR, ADAR1, DSRAD, G1P1, IFI4
Sequence domains:
DNA (5'-D(*TP*CP*GP*CP*GP*CP*G)-3') Chains: D, E
Molecule details ›
Chains: D, E
Length: 7 nucleotides
Theoretical weight: 2.11 KDa

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: P21
Unit cell:
a: 31.135Å b: 47.305Å c: 57.118Å
α: 90° β: 98.41° γ: 90°
R-values:
R R work R free
0.224 0.223 0.248
Expression system: Escherichia coli

Quick links

Citations

5 citation in other articles

Searching for New Z-DNA/Z-RNA Binding Proteins Based on Structural Similarity to Experimentally Validated Zα Domain.
Bartas et al. (2022)
4 more

1 mention without citation

Dual conformational recognition by Z-DNA binding protein is important for the B-Z transition process.
Park et al. (2020)