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

Structure

x-ray diffraction · 2 distinct chains · 48% helix, 23% strand (DSSP).

Ligands and binding sites

• UX0 · (1S,2R,3R,5R)-3-(hydroxymethyl)-5-((5-methoxyquinazolin-4-yl)amino)cyclopentane-1,2-diol · ligand · chains A
• MG · Magnesium ion · metal · chains B
• GOL · Glycerol · additive · 9 copies · chains A, B
• DMS · Dimethyl sulfoxide · additive · 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

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

Interfaces

1 interface between chains.

• A–B · 972 Ų buried · 25 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

• 5AQU · 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 5AQU · PDBe 5AQU · UniProt P11142 · UniProt Q99933