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Actin filament pointed end

Analyse Actin filament pointed end in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2Y83
Type
protein
Length
2,250 residues
Chains
6
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Actin, alpha skeletal muscle
UniProt
P68135
Ligands
ADP, CA
Pockets
19 · best druggability 0.80

Structure

electron microscopy · 1 distinct chain · 37% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
O, P, Q, R, S, TActin, alpha skeletal muscleprotein37537% helix, 16% strandP68135

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 6 copies · chains O, P, Q, R, S, T
  • CA · Calcium ion · metal · 6 copies · chains O, P, Q, R, S, T

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

Pockets

19 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13380.800.9059ADP, CA
210910.790.8093empty
39580.780.8093empty
48100.770.8167empty
59480.770.7970empty

Interfaces

9 interfaces between chains.

  • Q–S · 1205 Ų buried · 28 hydrogen bonds · protein-protein
  • O–Q · 1187 Ų buried · 23 hydrogen bonds · protein-protein
  • P–R · 1166 Ų buried · 23 hydrogen bonds · protein-protein
  • R–T · 1140 Ų buried · 19 hydrogen bonds · protein-protein
  • S–T · 970 Ų buried · 20 hydrogen bonds · protein-protein

Compared structures

  • 2Y83 · Actin filament pointed end · the same entry in another collection · chain T against T, TM-score 1.00
  • P68135 · AlphaFold monomer V2.0 prediction for actin, alpha skeletal muscle (P68135) · a predicted model of the same protein · chain P against A, TM-score 0.93

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