› 1f21

X-ray diffraction
1.4Å resolution

DIVALENT METAL COFACTOR BINDING IN THE KINETIC FOLDING TRAJECTORY OF E. COLI RIBONUCLEASE HI

Released:
DOI: 10.2210/pdb1f21/pdb
PDB entry 1f21 coloured by chain, front view.
PDB entry 1f21 coloured by chain, side view.
PDB entry 1f21 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Divalent metal cofactor binding in the kinetic folding trajectory of Escherichia coli ribonuclease HI.
Goedken ER, Keck JL, Berger JM, Marqusee S
Protein Sci 9 1914-21 (2000)
PMID: 11106164

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-141635 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease HI Chain: A
Molecule details ›
Chain: A
Length: 155 amino acids
Theoretical weight: 17.53 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A7Y4 (Residues: 1-155; Coverage: 100%)
Gene names: JW0204, b0214, dasF, herA, rnh, rnhA, sdrA
Sequence domains: RNase H
Structure domains: Ribonuclease H-like superfamily/Ribonuclease H

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 37.27Å b: 40.83Å c: 85.45Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.254
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Ribonuclease H evolution in retrotransposable elements.
Malik HS. (2005)
1 more

17 mentions without citation

What lessons can be learned from studying the folding of homologous proteins?
Nickson et al. (2010)
16 more