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Cryo-EM structure of F-ACTIN/PLASTIN2-ABD2 complex

Analyse Cryo-EM structure of F-ACTIN/PLASTIN2-ABD2 complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6VEC
Type
protein
Length
6,721 residues
Chains
22
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Actin, alpha skeletal muscle; LCP1
UniProt
P68135, V9HWJ7
Ligands
ADP, MG
Pockets
20 · best druggability 0.80

Structure

electron microscopy · 2 distinct chains · 48% helix, 12% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, KActin, alpha skeletal muscleprotein37043% helix, 20% strandP68135
a, b, c, d, e, f, g, h, i, j, kLCP1protein24156% helix, 0% strandV9HWJ7

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 11 copies · chains A, B, C, D, E, F, G, H, I, J, K
  • MG · Magnesium ion · metal · 11 copies · chains A, B, C, D, E, F, G, H, I, J, K

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

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13800.800.8955ADP, MG
28140.800.8387empty
33860.790.8855ADP, MG
43640.790.8953ADP, MG
54070.790.8859ADP, MG

Interfaces

39 interfaces between chains.

  • E–I · 1225 Ų buried · 13 hydrogen bonds · protein-protein
  • F–J · 1218 Ų buried · 13 hydrogen bonds · protein-protein
  • B–C · 1215 Ų buried · 9 hydrogen bonds · protein-protein
  • C–G · 1212 Ų buried · 12 hydrogen bonds · protein-protein
  • B–F · 1206 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 6VEC · Cryo-EM structure of F-actin/Plastin2-ABD2 complex · the same entry in another collection · chain K against K, TM-score 1.00

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