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Cryoem structure of myosin VI-actin complex in the ADP state

Analyse Cryoem structure of myosin VI-actin complex in the ADP state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6BNQ
Type
protein
Length
7,142 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Unconventional myosin-VI; Actin, alpha skeletal muscle
UniProt
F1RQI7, P68135
Ligands
ADP, MG
Pockets
20 · best druggability 0.83

Structure

electron microscopy · 2 distinct chains · 40% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
I, J, K, L, M, NUnconventional myosin-VIprotein70142% helix, 15% strandF1RQI7
A, B, C, D, E, F, G, HActin, alpha skeletal muscleprotein36738% helix, 20% strandP68135

Ligands and binding sites

  • ADP · Adenosine-5'-diphosphate · ligand · 8 copies · chains A, B, C, D, E, F, G, H
  • MG · Magnesium ion · metal · 8 copies · chains A, B, C, D, E, F, G, H

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
110410.830.8484empty
28900.830.8588empty
310900.830.84118empty
410530.830.84102empty
55510.820.8862empty

Interfaces

27 interfaces between chains.

  • E–G · 1190 Ų buried · 17 hydrogen bonds · protein-protein
  • I–C · 1184 Ų buried · 15 hydrogen bonds · protein-protein
  • K–E · 1163 Ų buried · 17 hydrogen bonds · protein-protein
  • N–H · 1159 Ų buried · 15 hydrogen bonds · protein-protein
  • D–F · 1150 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 6BNQ · CryoEM structure of Myosin VI-Actin complex in the ADP state · the same entry in another collection · chain A against A, TM-score 1.00

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