› 6gr5

X-ray diffraction
1.34Å resolution

Structure of human Heat shock protein 90-alpha N-terminal domain (Hsp90-NTD) variant K112R in complex with ADP

Released:
DOI: 10.2210/pdb6gr5/pdb
PDB entry 6gr5 coloured by chain, front view.
PDB entry 6gr5 coloured by chain, side view.
PDB entry 6gr5 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Probing the role of Arg97 in Heat shock protein 90 N-terminal domain from the parasite Leishmania braziliensis through site-directed mutagenesis on the human counterpart.
Tassone G, Mangani S, Botta M, Pozzi C
Biochim Biophys Acta Proteins Proteom 1866 1190-1198 (2018)
PMID: 30248409

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: 256 amino acids
Theoretical weight: 28.8 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P07900 (Residues: 1-236; Coverage: 32%)
Gene names: HSP90A, HSP90AA1, HSPC1, HSPCA
Sequence domains: Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P21
Unit cell:
a: 53.917Å b: 44.729Å c: 54.108Å
α: 90° β: 115.54° γ: 90°
R-values:
R R work R free
0.137 0.135 0.169
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

2 citation in other articles

Cordycepin (3'-Deoxyadenosine) Suppresses Heat Shock Protein 90 Function and Targets Tumor Growth in an Adenosine Deaminase-Dependent Manner.
Lee et al. (2022)
1 more

1 mention without citation

Integrating Network Pharmacology and Transcriptomic Strategies to Explore the Pharmacological Mechanism of Hydroxysafflor Yellow A in Delaying Liver Aging.
Kong et al. (2022)