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MolNFT v1 · #138461 · protein

Cryo-EM structure of B. subtilis flagellar filaments N226Y

5WJT · Flagellin: “Cryo-EM structure of B. subtilis flagellar filaments N226Y”. Electron microscopy, 20 pockets (best druggability 0.88). MolNFT v1 #138461 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
5WJT
Type
protein
Length
12,382 residues
Chains
41
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Flagellin
UniProt
A0A162QQD4
Pockets
20 · best druggability 0.88

Structure

electron microscopy · 1 distinct chain · 62% helix, 3% 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, h, i, j, k, l, m, n, oFlagellinprotein30262% helix, 3% strandA0A162QQD4

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19620.880.90133empty
27800.860.90106empty
37000.860.9093empty
47320.860.9092empty
56660.860.9090empty

Interfaces

126 interfaces between chains.

  • c–m · 2023 Ų buried · 20 hydrogen bonds · protein-protein
  • C–H · 2020 Ų buried · 20 hydrogen bonds · protein-protein
  • S–c · 2020 Ų buried · 20 hydrogen bonds · protein-protein
  • J–T · 2019 Ų buried · 20 hydrogen bonds · protein-protein
  • Z–j · 2019 Ų buried · 20 hydrogen bonds · protein-protein

Compared structures

  • 5WJT · Cryo-EM structure of B. subtilis flagellar filaments N226Y · the same entry in another collection · chain B against B, TM-score 1.00

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