› 5aqx

X-ray diffraction
2.12Å resolution

Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site residues

Released:
DOI: 10.2210/pdb5aqx/pdb
PDB entry 5aqx coloured by chain, front view.
PDB entry 5aqx coloured by chain, side view.
PDB entry 5aqx coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
A fragment-based approach applied to a highly flexible target: Insights and challenges towards the inhibition of HSP70 isoforms.
Jones AM, Westwood IM, Osborne JD, Matthews TP, Cheeseman MD, Rowlands MG, Jeganathan F, Burke R, Lee D, Kadi N, Liu M, Richards M, McAndrew C, Yahya N, Dobson SE, Jones K, Workman P, Collins I, van Montfort RL
Sci Rep 6 34701 (2016)
PMID: 27708405

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

3 bound ligands:
Ligand KC7 1 x KC7
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 I02
Spacegroup: P212121
Unit cell:
a: 51.845Å b: 82.021Å c: 94.421Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.227
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

Choose and Use Your Chemical Probe Wisely to Explore Cancer Biology.
Blagg et al. (2017)
3 more

1 mention without citation

A fragment-based approach applied to a highly flexible target: Insights and challenges towards the inhibition of HSP70 isoforms.
Jones et al. (2016)