› 5ar0

X-ray diffraction
1.9Å resolution

HSP72 with adenosine-derived inhibitor

Released:
DOI: 10.2210/pdb5ar0/pdb
PDB entry 5ar0 coloured by chain, front view.
PDB entry 5ar0 coloured by chain, side view.
PDB entry 5ar0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Exploiting Protein Conformational Change to Optimize Adenosine-Derived Inhibitors of HSP70.
Cheeseman MD, Westwood IM, Barbeau O, Rowlands M, Dobson S, Jones AM, Jeganathan F, Burke R, Kadi N, Workman P, Collins I, van Montfort RL, Jones K
J Med Chem 59 4625-36 (2016)
PMID: 27119979

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-143649 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock 70 kDa protein 1A Chain: A
Molecule details ›
Chain: A
Length: 394 amino acids
Theoretical weight: 43.2 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0DMV8 (Residues: 1-380; Coverage: 59%)
Gene names: HSP72, HSPA1, HSPA1A, HSX70
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand GB8 1 x GB8
Ligand GOL 3 x GOL
Ligand DMS 2 x DMS
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I24
Spacegroup: P212121
Unit cell:
a: 47.88Å b: 80.545Å c: 92.979Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.174 0.172 0.21
Expression system: Escherichia coli BL21

Quick links

Citations

5 review citations

HSP70 Multi-Functionality in Cancer.
Albakova et al. (2020)
4 more

2 mentions without citation

Exploiting Protein Conformational Change to Optimize Adenosine-Derived Inhibitors of HSP70.
Cheeseman et al. (2016)
1 more