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Structure of the bacterial flagellar polyrod

Analyse Structure of the bacterial flagellar polyrod in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6JZR
Type
protein
Length
5,434 residues
Chains
22
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Flagellar basal-body rod protein flgg
UniProt
A0A0J5DTL8
Pockets
20 · best druggability 0.90

Structure

electron microscopy · 1 distinct chain · 24% helix, 26% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, K, a, b, c, d, e, f, g, h, i, j, kFlagellar basal-body rod protein flggprotein24724% helix, 26% strandA0A0J5DTL8

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19810.900.92130empty
211010.900.92149empty
310840.890.90132empty
44970.870.9378empty
54310.870.9465empty

Interfaces

83 interfaces between chains.

  • J–d · 2229 Ų buried · 33 hydrogen bonds · protein-protein
  • d–i · 2225 Ų buried · 33 hydrogen bonds · protein-protein
  • A–F · 2224 Ų buried · 33 hydrogen bonds · protein-protein
  • I–c · 2223 Ų buried · 33 hydrogen bonds · protein-protein
  • F–K · 2222 Ų buried · 33 hydrogen bonds · protein-protein

Compared structures

  • 6JZR · Structure of the bacterial flagellar polyrod · the same entry in another collection · chain C against C, TM-score 1.00

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