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The yeast actin val 159 asn mutant complex with human gelsolin segment 1.

Analyse The yeast actin val 159 asn mutant complex with human gelsolin segment 1. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1YVN
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 0.72

Structure

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

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (actin)protein37244% 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
13200.720.8537empty
24000.710.8354MG, ATP
31610.450.7521empty
4750.300.7418empty

Interfaces

1 interface between chains.

  • A–G · 1046 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 1YVN · The yeast actin val 159 asn mutant complex with human gelsolin segment 1. · 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

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