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The baseplate complex from the type VI secretion system

Analyse The baseplate complex from the type VI secretion system in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6GIY
Type
protein
Length
3,649 residues
Chains
9
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Tssf; Tssg; Tssk
UniProt
B7LFT7, B7LFT6, B7LG64
Pockets
20 · best druggability 0.89

Structure

electron microscopy · 5 distinct chains · 24% helix, 14% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ATssfprotein58417% helix, 10% strandB7LFT7
BTssfprotein58324% helix, 11% strandB7LFT7
CTssgprotein35028% helix, 7% strandB7LFT6
D, E, F, ITsskprotein31129% helix, 21% strandB7LG64
G, HTsskprotein44426% helix, 23% strandB7LG64

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18250.890.91129empty
211180.880.90140empty
311760.870.88134empty
46320.870.9181empty
59330.870.88113empty

Interfaces

21 interfaces between chains.

  • B–C · 3305 Ų buried · 23 hydrogen bonds · protein-protein
  • A–C · 3273 Ų buried · 20 hydrogen bonds · protein-protein
  • G–H · 2990 Ų buried · 32 hydrogen bonds · protein-protein
  • D–F · 2926 Ų buried · 22 hydrogen bonds · protein-protein
  • G–I · 2868 Ų buried · 24 hydrogen bonds · protein-protein

Compared structures

  • 6GIY · The baseplate complex from the type VI secretion system · the same entry in another collection · chain A against A, TM-score 1.00

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