› 3opd

X-ray diffraction
2.6Å resolution

Crystal Structure of the N-terminal domain of an HSP90 from Trypanosoma Brucei, Tb10.26.1080 in the presence of a benzamide derivative

Released:
DOI: 10.2210/pdb3opd/pdb
PDB entry 3opd coloured by chain, front view.
PDB entry 3opd coloured by chain, side view.
PDB entry 3opd coloured by chain, top view.
Source organism: Trypanosoma brucei brucei
Primary publication:
Exploring the Trypanosoma brucei Hsp83 potential as a target for structure guided drug design.
Pizarro JC, Hills T, Senisterra G, Wernimont AK, Mackenzie C, Norcross NR, Ferguson MA, Wyatt PG, Gilbert IH, Hui R
PLoS Negl Trop Dis 7 e2492 (2013)
PMID: 24147171

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-146346 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein 83 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 231 amino acids
Theoretical weight: 26.2 KDa
Source organism: Trypanosoma brucei brucei
Expression system: Escherichia coli
UniProt:
  • Canonical: P12861 (Residues: 1-213; Coverage: 30%)
Gene name: HSP83
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

1 bound ligand:
Ligand HIE 3 x HIE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 70.915Å b: 72.103Å c: 152.147Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.186 0.247
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Elucidating drug resistance in human fungal pathogens.
Xie et al. (2014)
3 more

4 mentions without citation

Structural Basis of Parasitic HSP90 ATPase Inhibition by Small Molecules.
Tassone et al. (2022)
3 more