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DHF38 filament

Analyse DHF38 filament in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6E9Y
Type
protein
Length
3,405 residues
Chains
15
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
DHF38 filament
Pockets
20 · best druggability 0.78

Structure

electron microscopy · 1 distinct chain · 91% helix, 0% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, L, M, N, ODHF38 filamentprotein22791% helix, 0% strand—

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111630.780.80129empty
210000.750.7890empty
311370.750.78105empty
410570.750.7895empty
510490.750.7899empty

Interfaces

35 interfaces between chains.

  • A–J · 900 Ų buried · 16 hydrogen bonds · protein-protein
  • F–I · 898 Ų buried · 16 hydrogen bonds · protein-protein
  • K–O · 895 Ų buried · 16 hydrogen bonds · protein-protein
  • A–C · 895 Ų buried · 16 hydrogen bonds · protein-protein
  • B–F · 895 Ų buried · 16 hydrogen bonds · protein-protein

Compared structures

  • 6E9Y · DHF38 filament · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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