› 1i39

X-ray diffraction
1.95Å resolution

RNASE HII FROM ARCHAEOGLOBUS FULGIDUS

Released:
DOI: 10.2210/pdb1i39/pdb
PDB entry 1i39 coloured by chain, front view.
PDB entry 1i39 coloured by chain, side view.
PDB entry 1i39 coloured by chain, top view.
Source organism: Archaeoglobus fulgidus
Primary publication:
Structural biochemistry of a type 2 RNase H: RNA primer recognition and removal during DNA replication.
Chapados BR, Chai Q, Hosfield DJ, Qiu J, Shen B, Tainer JA
J Mol Biol 307 541-56 (2001)
PMID: 11254381

Function and Biology Details

Reaction catalysed: 
Endonucleolytic cleavage to 5'-phosphomonoester.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128153 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease HII Chain: A
Molecule details ›
Chain: A
Length: 225 amino acids
Theoretical weight: 25.39 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O29634 (Residues: 1-205; Coverage: 100%)
Gene names: AF_0621, rnhB
Sequence domains: Ribonuclease HII
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-1
Spacegroup: P6522
Unit cell:
a: 74.826Å b: 74.826Å c: 142.747Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.244 0.244 0.269
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

Ribonuclease H: molecular diversities, substrate binding domains, and catalytic mechanism of the prokaryotic enzymes.
Tadokoro et al. (2009)
7 more

4 mentions without citation

PCNA directs type 2 RNase H activity on DNA replication and repair substrates.
Bubeck et al. (2011)
3 more