› 6gfa

X-ray diffraction
2Å resolution

Structure of Nucleotide binding domain of HSP110, ATP and Mg2+ complexed

Released:
DOI: 10.2210/pdb6gfa/pdb
PDB entry 6gfa coloured by chain, front view.
PDB entry 6gfa coloured by chain, side view.
PDB entry 6gfa coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Selecting the first chemical molecule inhibitor of HSP110 for colorectal cancer therapy.
Gozzi GJ, Gonzalez D, Boudesco C, Dias AMM, Gotthard G, Uyanik B, Dondaine L, Marcion G, Hermetet F, Denis C, Hardy L, Suzanne P, Douhard R, Jego G, Dubrez L, Demidov ON, Neiers F, Briand L, Sopková-de Oliveira Santos J, Voisin-Chiret AS, Garrido C
Cell Death Differ 27 117-129 (2020)
PMID: 31068676

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-187703 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Heat shock protein 105 kDa Chain: A
Molecule details ›
Chain: A
Length: 381 amino acids
Theoretical weight: 42.19 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q92598 (Residues: 1-381; Coverage: 44%)
Gene names: HSP105, HSP110, HSPH1, KIAA0201
Sequence domains: Hsp70 protein
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand ATP 1 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P6122
Unit cell:
a: 109.78Å b: 109.78Å c: 144.22Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.187 0.229
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

10 review citations

Heat-shock proteins: chaperoning DNA repair.
Dubrez et al. (2020)
9 more

4 mentions without citation

Amyloid management by chaperones: The mystery underlying protein oligomers' dual functions.
Arghavani et al. (2022)
3 more