› 1ecl

X-ray diffraction
1.9Å resolution

AMINO TERMINAL 67KDA DOMAIN OF ESCHERICHIA COLI DNA TOPOISOMERASE I (RESIDUES 2-590 OF MATURE PROTEIN) CLONING ARTIFACT ADDS TWO RESIDUES TO THE AMINO-TERMINUS WHICH WERE NOT OBSERVED IN THE EXPERIMENTAL ELECTRON DENSITY (GLY-2, SER-1).

Released:
DOI: 10.2210/pdb1ecl/pdb
PDB entry 1ecl coloured by chain, front view.
PDB entry 1ecl coloured by chain, side view.
PDB entry 1ecl coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I.
Lima CD, Wang JC, Mondragón A
Nature 367 138-46 (1994)
PMID: 8114910

Function and Biology Details

Reaction catalysed: 
ATP-independent breakage of single-stranded DNA, followed by passage and rejoining
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139094 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
DNA topoisomerase 1 Chain: A
Molecule details ›
Chain: A
Length: 597 amino acids
Theoretical weight: 67.33 KDa
Source organism: Escherichia coli
Expression system: Not provided
UniProt:
  • Canonical: P06612 (Residues: 1-597; Coverage: 69%)
Gene names: JW1266, b1274, supX, topA
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS
Spacegroup: P212121
Unit cell:
a: 63.19Å b: 77.97Å c: 138.9Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.218 0.218 not available
Expression system: Not provided

Quick links

Citations

42 review citations

DNA topoisomerases: structure, function, and mechanism.
Champoux JJ. (2001)
41 more

20 mentions without citation

Mechanism of Type IA Topoisomerases.
Dasgupta et al. (2020)
19 more