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

Structure

x-ray diffraction · 4 distinct chains · 48% helix, 22% strand (DSSP).

Ligands and binding sites

• ADN · Adenosine · ligand · 2 copies · chains A, C
• GOL · Glycerol · additive · 12 copies · chains A, B, C, D
• TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · 2 copies · chains A, C

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

Pockets

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

Interfaces

5 interfaces between chains.

• A–B · 1049 Ų buried · 24 hydrogen bonds · protein-protein
• C–D · 989 Ų buried · 22 hydrogen bonds · protein-protein
• B–D · 119 Ų buried · 2 hydrogen bonds · protein-protein
• A–C · 102 Ų buried · 0 hydrogen bonds · protein-protein
• A–D · 47 Ų buried · 0 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

• 5AQF · Fragment-based screening of HSP70 sheds light on the functional role of ATP-binding site… · the same entry in another collection · chain D against D, 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 D against A, TM-score 0.91
• 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 0.82

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 5AQF · PDBe 5AQF · UniProt P11142 · UniProt Q99933