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Cryoem structure of myosinvi-actin complex in the rigor (nucleotide- free) state

Analyse Cryoem structure of myosinvi-actin complex in the rigor (nucleotide- free) state in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6BNP
Type
protein
Length
7,160 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 · 41% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
I, J, K, L, M, NUnconventional myosin-VIprotein70442% helix, 16% strandF1RQI7
A, B, C, D, E, F, G, HActin, alpha skeletal muscleprotein36740% helix, 21% 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
17040.830.8779empty
211440.830.84106empty
37850.820.8593empty
45190.820.8862empty
58920.810.8494empty

Interfaces

26 interfaces between chains.

  • A–C · 1193 Ų buried · 14 hydrogen bonds · protein-protein
  • K–E · 1173 Ų buried · 17 hydrogen bonds · protein-protein
  • E–G · 1166 Ų buried · 12 hydrogen bonds · protein-protein
  • B–D · 1154 Ų buried · 12 hydrogen bonds · protein-protein
  • F–H · 1152 Ų buried · 13 hydrogen bonds · protein-protein

Compared structures

  • 6BNP · CryoEM structure of MyosinVI-actin complex in the rigor (nucleotide-free) state · the same entry in another collection · chain N against N, TM-score 1.00

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