› 1ecs

X-ray diffraction
1.7Å resolution

THE 1.7 A CRYSTAL STRUCTURE OF A BLEOMYCIN RESISTANCE DETERMINANT ENCODED ON THE TRANSPOSON TN5

Released:
DOI: 10.2210/pdb1ecs/pdb
PDB entry 1ecs coloured by chain, front view.
PDB entry 1ecs coloured by chain, side view.
PDB entry 1ecs coloured by chain, top view.
Source organism: Klebsiella pneumoniae
Primary publication:
Crystal structures of the transposon Tn5-carried bleomycin resistance determinant uncomplexed and complexed with bleomycin.
Maruyama M, Kumagai T, Matoba Y, Hayashida M, Fujii T, Hata Y, Sugiyama M
J Biol Chem 276 9992-9 (2001)
PMID: 11134052

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146466 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Bleomycin resistance protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 126 amino acids
Theoretical weight: 14.01 KDa
Source organism: Klebsiella pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: P13081 (Residues: 1-126; Coverage: 100%)
Gene name: ble
Sequence domains: Glyoxalase/Bleomycin resistance protein/Dioxygenase superfamily
Structure domains: 2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1

Ligands and Environments

2 bound ligands:
Ligand CA 1 x CA
Ligand PG4 2 x PG4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-18B
Spacegroup: C2221
Unit cell:
a: 81.33Å b: 85.03Å c: 78.82Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.191 not available not available
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Structural biological study of self-resistance determinants in antibiotic-producing actinomycetes.
Sugiyama M. (2015)
2 more

4 mentions without citation

Expression of Xhdsi-1VOC, a novel member of the vicinal oxygen chelate (VOC) metalloenzyme superfamily, is up-regulated in leaves and roots during desiccation in the resurrection plant Xerophyta humilis (Bak) Dur and Schinz.
Mulako et al. (2008)
3 more