Crystal structure of the C-terminal calponin homology domain of alpha- parvin in complex with paxillin LD2 motif

Structure

x-ray diffraction · 2 distinct chains · 65% helix, 0% strand (DSSP).

Ligands and binding sites

• EDO · 1,2-ethanediol · additive · 5 copies · chains B
• PG4 · Tetraethylene glycol · additive · chains B
• PGE · Triethylene glycol · additive · chains B

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Interfaces

1 interface between chains.

• A–B · 516 Ų buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (additive adduct).

Compared structures

• 2VZG · Crystal structure of the C-terminal calponin homology domain of alpha- parvin in complex… · the same entry in another collection · chain A against A, 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 A against A, TM-score 0.64

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