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33MER structure of the salmonella flagella ms-ring protein flif

Analyse 33MER structure of the salmonella flagella ms-ring protein flif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SCN
Type
protein
Length
7,875 residues
Chains
33
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Flagellar M-ring protein
UniProt
A0A0D6FLL5
Pockets
20 · best druggability 0.84

Structure

electron microscopy · 2 distinct chains · 29% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, L, M, N, O, P, Q, R, S, T, U, W, X, Y, Z, a, b, c, d, e, fFlagellar M-ring proteinprotein24730% helix, 33% strandA0A0D6FLL5
K, V, gFlagellar M-ring proteinprotein15526% helix, 41% strandA0A0D6FLL5

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18250.840.87101empty
211730.820.83122empty
39960.820.83100empty
49590.810.83102empty
510270.810.8399empty

Interfaces

45 interfaces between chains.

  • Q–R · 3483 Ų buried · 67 hydrogen bonds · protein-protein
  • F–G · 3477 Ų buried · 67 hydrogen bonds · protein-protein
  • b–c · 3474 Ų buried · 69 hydrogen bonds · protein-protein
  • C–D · 3444 Ų buried · 59 hydrogen bonds · protein-protein
  • Y–Z · 3403 Ų buried · 59 hydrogen bonds · protein-protein

Compared structures

  • 6SCN · 33mer structure of the Salmonella flagella MS-ring protein FliF · the same entry in another collection · chain B against B, TM-score 1.00

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