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

Structure

x-ray diffraction · 2 distinct chains · 49% helix, 22% strand (DSSP).

Ligands and binding sites

• KC7 · (1R,2S,3R,5R)-3-((5-(benzyloxy)quinazolin-4-yl)amino)-5-(hydroxymethyl)cyclopentane-1,2-diol · ligand · chains A
• GOL · Glycerol · additive · 7 copies · chains A, B
• DMS · Dimethyl sulfoxide · additive · 3 copies · chains A
• TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 1003 Ų buried · 26 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

• 5AQV · Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site… · the same entry in another collection · chain A against A, TM-score 1.00
• Q99933 · AlphaFold monomer V2.0 prediction for bag family molecular chaperone regulator 1 (Q99933) · a predicted model of the same protein · chain B against A, TM-score 0.95
• P11142 · AlphaFold monomer V2.0 prediction for heat shock cognate 71 kda protein (P11142) · a predicted model of the same protein · chain A against A, TM-score 0.83

Analyse

• Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
• Every structure of UniProt P11142
• Every structure of UniProt Q99933
• Elsewhere: RCSB PDB 5AQV · PDBe 5AQV · UniProt P11142 · UniProt Q99933