› 3qtf

X-ray diffraction
1.57Å resolution

Design and SAR of macrocyclic Hsp90 inhibitors with increased metabolic stability and potent cell-proliferation activity

Released:
DOI: 10.2210/pdb3qtf/pdb
PDB entry 3qtf coloured by chain, front view.
PDB entry 3qtf coloured by chain, side view.
PDB entry 3qtf coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Design and SAR of macrocyclic Hsp90 inhibitors with increased metabolic stability and potent cell-proliferation activity.
Zapf CW, Bloom JD, McBean JL, Dushin RG, Nittoli T, Ingalls C, Sutherland AG, Sonye JP, Eid CN, Golas J, Liu H, Boschelli F, Hu Y, Vogan E, Levin JI
Bioorg Med Chem Lett 21 2278-82 (2011)
PMID: 21420297

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139817 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein HSP 90-alpha Chain: A
Molecule details ›
Chain: A
Length: 226 amino acids
Theoretical weight: 25.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07900 (Residues: 10-236; Coverage: 31%)
Gene names: HSP90A, HSP90AA1, HSPC1, HSPCA
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase
Structure domains: Histidine kinase-like ATPase, C-terminal domain

Ligands and Environments

2 bound ligands:
Ligand 05S 1 x 05S
Ligand DMS 1 x DMS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU FR-E+ SUPERBRIGHT
Spacegroup: I222
Unit cell:
a: 67.264Å b: 90.718Å c: 98.379Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.187 0.204
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 review citations

Macrocyclic drugs and synthetic methodologies toward macrocycles.
Yu et al. (2013)
1 more