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Cryo-EM structure of escrt-III helical VPS24 filaments

Analyse Cryo-EM structure of escrt-III helical VPS24 filaments in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6ZH3
Type
protein
Length
680 residues
Chains
4
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Vacuolar protein-sorting-associated protein 24
UniProt
P36095
Pockets
7 · best druggability 0.35

Structure

electron microscopy · 1 distinct chain · 78% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
B, A, C, DVacuolar protein-sorting-associated protein 24protein17078% helix, 0% strandP36095

Pockets

7 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
1740.350.7715empty
2740.330.7515empty
3750.330.7518empty
4800.320.7414empty
5690.320.7515empty

Interfaces

3 interfaces between chains.

  • B–A · 3360 Ų buried · 26 hydrogen bonds · protein-protein
  • C–D · 3352 Ų buried · 28 hydrogen bonds · protein-protein
  • B–C · 53 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 6ZH3 · Cryo-EM structure of ESCRT-III helical Vps24 filaments · the same entry in another collection · chain B against B, TM-score 1.00
  • P36095 · AlphaFold monomer V2.0 prediction for vacuolar protein-sorting- associated protein 24… · a predicted model of the same protein · chain B against A, TM-score 0.49

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