Protein-ligand interactions: thermodynamic effects associated with increasing hydrophobic surface area

Structure

x-ray diffraction · 2 distinct chains · 14% helix, 27% strand (DSSP).

Ligands and binding sites

• ACE · Acetyl group · ligand · chains A, B
• NH2 · Amino group · ion · chains A, B
• CL · Chloride ion · ion · chains A
• GOL · Glycerol · additive · chains A

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

Interfaces

1 interface between chains.

• A–B · 395 Ų buried · 11 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 modified, 1 covalent (covalent ligand, nonstandard, phosphorylation).

Compared structures

• 3S8L · Protein-Ligand Interactions: Thermodynamic Effects Associated with Increasing Hydrophobic… · the same entry in another collection · chain A against A, TM-score 1.00
• P62993 · AlphaFold monomer V2.0 prediction for growth factor receptor-bound protein 2 (P62993) · a predicted model of the same protein · chain A against A, TM-score 0.95

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 P62993
• Elsewhere: RCSB PDB 3S8L · PDBe 3S8L · UniProt P62993