Structure, thermodynamics, and the role of conformational dynamics in the interactions between the N-terminal SH3 domain of crkii and proline-rich motifs in cabl

Structure

x-ray diffraction · 3 distinct chains · 5% helix, 42% strand (DSSP).

Ligands and binding sites

• ACE · Acetyl group · ligand · 2 copies · chains A, M, N
• P4G · 1-ethoxy-2-(2-ethoxyethoxy)ethane · ligand · 2 copies · chains A, B, N
• NA · Sodium ion · metal · 4 copies · chains A, B
• NH2 · Amino group · ion · 2 copies · chains M, B, N
• PEG · Di(hydroxyethyl)ether · additive · chains A

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

Interfaces

3 interfaces between chains.

• A–M · 522 Ų buried · 7 hydrogen bonds · protein-protein
• B–N · 485 Ų buried · 8 hydrogen bonds · protein-protein
• A–B · 371 Ų buried · 10 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 covalent (covalent ligand).

Compared structures

• 5IH2 · Structure, thermodynamics, and the role of conformational dynamics in the interactions… · the same entry in another collection · chain A against A, TM-score 1.00
• Q64010 · AlphaFold monomer V2.0 prediction for adapter molecule crk (Q64010) · a predicted model of the same protein · chain B against A, TM-score 0.96

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 Q64010
• Elsewhere: RCSB PDB 5IH2 · PDBe 5IH2 · UniProt Q64010