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Structure of the yeast actin-human gelsolin segment 1 complex

Analyse Structure of the yeast actin-human gelsolin segment 1 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1YAG
Type
protein
Length
497 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (actin); Protein (gelsolin)
UniProt
P60010, P06396
Ligands
ATP, MG, CA, SO4
Pockets
4 · best druggability 0.73

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (actin)protein37243% helix, 20% strandP60010
GProtein (gelsolin)protein12523% helix, 34% strandP06396

Ligands and binding sites

  • ATP · Adenosine-5'-triphosphate · ligand · chains A
  • MG · Magnesium ion · metal · chains A
  • CA · Calcium ion · metal · chains G
  • SO4 · Sulfate ion · ion · chains A

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

Pockets

4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14200.730.8352MG, ATP
22870.710.8535empty
31620.450.7522empty
4680.290.7418empty

Interfaces

1 interface between chains.

  • A–G · 1057 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 1YAG · Structure of the yeast actin-human gelsolin segment 1 complex · the same entry in another collection · chain A against A, TM-score 1.00
  • P60010 · AlphaFold monomer V2.0 prediction for actin (P60010) · a predicted model of the same protein · chain A against A, TM-score 0.98
  • P06396 · AlphaFold monomer V2.0 prediction for gelsolin (P06396) · a predicted model of the same protein · chain G against A, TM-score 0.95

Analyse

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