› 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 1f21 coloured by chain and viewed from the front.
PDB 1f21 coloured by chain and viewed from the side.
PDB 1f21 coloured by chain and viewed from the top.
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)
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

Cofactor engineering for enhancing the flux of metabolic pathways.
Akhtar et al. (2014)
1 more

17 mentions without citation

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