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8T8P: 33-mer FliF MS-ring from Salmonella

Analyse 8T8P: 33-mer FliF MS-ring from Salmonella in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
8T8P
Type
protein
Length
9,009 residues
Chains
33
Method
electron microscopy
Authors
Singh, P.K., Iverson, T.M.
Deposited
06/23/23
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
3.4
Source
Salmonella enterica subsp. enterica serovar Typhimurium
Molecule
Flagellar M-ring protein
UniProt
P15928
Pockets
20 · best druggability 0.83

Structure

electron microscopy · resolution 3.4 · 2 distinct chains · 32% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, D, F, G, I, J, L, M, O, P, R, S, V, W, Y, Z, BA, CA, EA, FA, HAFlagellar M-ring proteinprotein25430% helix, 32% strandP15928
B, E, H, K, N, Q, T, X, AA, DA, GAFlagellar M-ring proteinprotein31134% helix, 26% strandP15928

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18550.830.86126empty
28660.810.84132empty
39270.800.82100empty
49730.800.82105empty
58910.790.8293empty

Interfaces

44 interfaces between chains.

  • C–FA · 3555 Ų buried · 58 hydrogen bonds · protein-protein
  • D–I · 3541 Ų buried · 61 hydrogen bonds · protein-protein
  • Z–EA · 3540 Ų buried · 58 hydrogen bonds · protein-protein
  • CA–HA · 3536 Ų buried · 59 hydrogen bonds · protein-protein
  • J–O · 3528 Ų buried · 58 hydrogen bonds · protein-protein

Compared structures

  • P15928 · AlphaFold monomer V2.0 prediction for flagellar M-ring protein (P15928) · a predicted model of the same protein · chain A against A, TM-score 0.70

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