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Crystal structure of the C-terminal calponin homology domain of alpha- parvin in complex with paxillin LD4 motif

Analyse Crystal structure of the C-terminal calponin homology domain of alpha- parvin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2VZI
Type
protein
Length
139 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
PAXILLIN,PAXILLIN; Alpha-parvin
UniProt
P49023, Q9NVD7

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
APAXILLIN,PAXILLINprotein1385% helix, 0% strandP49023
BAlpha-parvinprotein12663% helix, 0% strandQ9NVD7

Ligands and binding sites

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

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

Interfaces

1 interface between chains.

  • A–B · 508 Ų buried · 4 hydrogen bonds · protein-protein

Compared structures

  • 2VZI · 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 0.99
  • P49023 · AlphaFold monomer V2.0 prediction for paxillin (P49023) · a predicted model of the same protein · chain A against A, TM-score 0.78

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