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In situ assembled salmonella flgd hook cap complex

Analyse In situ assembled salmonella flgd hook cap complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7BHQ
Type
protein
Length
1,010 residues
Chains
5
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Basal-body rod modification protein flgd
UniProt
P0A1I9
Pockets
7 · best druggability 0.86

Structure

electron microscopy · 4 distinct chains · 26% helix, 36% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABasal-body rod modification protein flgdprotein20126% helix, 35% strandP0A1I9
B, EBasal-body rod modification protein flgdprotein20427% helix, 35% strandP0A1I9
CBasal-body rod modification protein flgdprotein19926% helix, 37% strandP0A1I9
DBasal-body rod modification protein flgdprotein20226% helix, 36% strandP0A1I9

Pockets

7 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111300.860.87103empty
23960.690.8155empty
3560.580.9118empty
4750.420.8015empty
5650.340.7713empty

Interfaces

6 interfaces between chains.

  • A–B · 1583 Ų buried · 14 hydrogen bonds · protein-protein
  • A–E · 1542 Ų buried · 19 hydrogen bonds · protein-protein
  • B–C · 1510 Ų buried · 11 hydrogen bonds · protein-protein
  • D–E · 1438 Ų buried · 12 hydrogen bonds · protein-protein
  • C–D · 1272 Ų buried · 12 hydrogen bonds · protein-protein

Compared structures

  • 7BHQ · In situ assembled Salmonella FlgD hook cap complex · the same entry in another collection · chain E against E, TM-score 1.00
  • P0A1I9 · AlphaFold monomer V2.0 prediction for basal-body rod modification protein flgd (P0A1I9) · a predicted model of the same protein · chain A against A, TM-score 0.78

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