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Thin filament at low calcium concentration

Analyse Thin filament at low calcium concentration in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5MVY
Type
protein
Length
8,625 residues
Chains
23
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Actin, alpha skeletal muscle
UniProt
P68135
Ligands
ADP
Pockets
20 · best druggability 0.85

Structure

electron microscopy · 1 distinct chain · 40% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, WActin, alpha skeletal muscleprotein37540% helix, 17% strandP68135

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 23 copies · chains A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P, Q, R, S, T, U, V, W

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
110310.850.86139ADP
29500.850.86139ADP
39370.850.86125ADP
49500.850.86135ADP
59160.850.86134ADP

Interfaces

43 interfaces between chains.

  • U–W · 917 Ų buried · 5 hydrogen bonds · protein-protein
  • S–U · 916 Ų buried · 5 hydrogen bonds · protein-protein
  • Q–S · 915 Ų buried · 5 hydrogen bonds · protein-protein
  • E–G · 915 Ų buried · 5 hydrogen bonds · protein-protein
  • F–H · 915 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 23 modified (methylation).

Compared structures

  • 5MVY · Thin Filament at low calcium concentration · the same entry in another collection · chain K against K, TM-score 1.00

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