Crystal structure of the C-terminal calponin homology domain of alpha parvin in complex with paxillin LD1 motif

Structure

x-ray diffraction · 4 distinct chains · 65% helix, 1% strand (DSSP).

Ligands and binding sites

• EDO · 1,2-ethanediol · additive · 7 copies · chains A, B
• GOL · Glycerol · additive · 3 copies · chains A, B
• PGE · Triethylene glycol · additive · 2 copies · chains A
• PG4 · Tetraethylene glycol · additive · 2 copies · chains A, B

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

3 interfaces between chains.

• B–D · 594 Ų buried · 5 hydrogen bonds · protein-protein
• A–B · 532 Ų buried · 4 hydrogen bonds · protein-protein
• A–C · 524 Ų buried · 5 hydrogen bonds · protein-protein

Compared structures

• 2VZD · Crystal structure of the C-terminal calponin homology domain of alpha parvin in complex… · the same entry in another collection · chain D against D, TM-score 1.00
• Q9NVD7 · AlphaFold monomer V2.0 prediction for alpha-parvin (Q9NVD7) · a predicted model of the same protein · chain B against A, TM-score 0.98
• P49023 · AlphaFold monomer V2.0 prediction for paxillin (P49023) · a predicted model of the same protein · chain C against A, TM-score 0.66

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 Q9NVD7
• Every structure of UniProt P49023
• Elsewhere: RCSB PDB 2VZD · PDBe 2VZD · UniProt Q9NVD7 · UniProt P49023