› 4io8

X-ray diffraction
2.58Å resolution

Crystal structure of human HSP70 complexed with 4-{(2R,3S,4R)-5-[(R)-6-Amino-8-(3,4-dichloro-benzylamino)-purin-9-yl]-3,4-dihydroxy-tetrahydro-furan-2-ylmethoxymethyl}-benzonitrile

Released:
DOI: 10.2210/pdb4io8/pdb
PDB entry 4io8 coloured by chain, front view.
PDB entry 4io8 coloured by chain, side view.
PDB entry 4io8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Functional analysis of Hsp70 inhibitors.
Schlecht R, Scholz SR, Dahmen H, Wegener A, Sirrenberg C, Musil D, Bomke J, Eggenweiler HM, Mayer MP, Bukau B
PLoS One 8 e78443 (2013)
PMID: 24265689

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: 382 amino acids
Theoretical weight: 42.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P0DMV8 (Residues: 1-382; Coverage: 60%)
Gene names: HSP72, HSPA1, HSPA1A, HSX70
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21
Unit cell:
a: 58.68Å b: 53.973Å c: 70.796Å
α: 90° β: 101.07° γ: 90°
R-values:
R R work R free
0.172 0.169 0.222
Expression system: Escherichia coli

Quick links

Citations

18 review citations

The human HSP70 family of chaperones: where do we stand?
Radons J. (2016)
17 more

8 mentions without citation

Targeting Allosteric Control Mechanisms in Heat Shock Protein 70 (Hsp70).
Li et al. (2016)
7 more