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34-fold symmetry salmonella S ring formed by full-length flif

Analyse 34-fold symmetry salmonella S ring formed by full-length flif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7D84
Type
protein
Length
5,406 residues
Chains
34
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Flagellar M-ring protein
UniProt
P15928
Pockets
20 · best druggability 0.73

Structure

electron microscopy · 1 distinct chain · 30% helix, 35% 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, W, X, Y, Z, a, b, c, d, e, f, g, hFlagellar M-ring proteinprotein15930% helix, 35% strandP15928

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13520.730.8538empty
23640.730.8437empty
33500.730.8436empty
43770.730.8437empty
53610.730.8436empty

Interfaces

34 interfaces between chains.

  • D–E · 2418 Ų buried · 34 hydrogen bonds · protein-protein
  • J–K · 2414 Ų buried · 34 hydrogen bonds · protein-protein
  • R–S · 2414 Ų buried · 34 hydrogen bonds · protein-protein
  • L–M · 2413 Ų buried · 34 hydrogen bonds · protein-protein
  • e–f · 2413 Ų buried · 34 hydrogen bonds · protein-protein

Compared structures

  • 7D84 · 34-fold symmetry Salmonella S ring formed by full-length FliF · the same entry in another collection · chain H against H, TM-score 1.00

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