› 3u67

X-ray diffraction
1.77Å resolution

Crystal structure of the N-terminal domain of Hsp90 from Leishmania major(LmjF33.0312)in complex with ADP

Released:
DOI: 10.2210/pdb3u67/pdb
PDB entry 3u67 coloured by chain, front view.
PDB entry 3u67 coloured by chain, side view.
PDB entry 3u67 coloured by chain, top view.
Source organism: Leishmania major strain Friedlin
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

Assemblies composition:
monomeric (preferred)
homo dimer
Assembly name:
PDBe Complex ID:
PDB-CPX-175673 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Histidine kinase/HSP90-like ATPase domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 231 amino acids
Theoretical weight: 26.11 KDa
Source organism: Leishmania major strain Friedlin
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q4Q4I6 (Residues: 1-213; Coverage: 30%)
Gene names: HSP83, HSP83-10, HSP83-11, HSP83-12, HSP83-13, HSP83-14, HSP83-15, HSP83-16, HSP83-17, HSP83-2, HSP83-3, HSP83-5, HSP83-6, HSP83-7, HSP83-9, LMJF_33_0312, LMJF_33_0314, LMJF_33_0316, LMJF_33_0320, LMJF_33_0323, LMJF_33_0326, LMJF_33_0333, LMJF_33_0336, LMJF_33_0340, LMJF_33_0343, LMJF_33_0346, LMJF_33_0350, LMJF_33_0355, LMJF_33_0360, LMJF_33_0365
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

3 bound ligands:
Ligand ADP 1 x ADP
Ligand MG 1 x MG
Ligand EDO 3 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007
Spacegroup: P21212
Unit cell:
a: 121.865Å b: 42.991Å c: 51.253Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.202 0.24
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

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

4 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
3 more