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Arches protomer (trimer of TRWG/VIRB8PERI) structure from the fully- assembled R388 type IV secretion system determined by cryo-EM.

Analyse Arches protomer (trimer of TRWG/VIRB8PERI) structure from the fully- assembled… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7Q1V
Type
protein
Length
411 residues
Chains
3
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Trwg protein
UniProt
O50335
Pockets
3 · best druggability 0.60

Structure

electron microscopy · 1 distinct chain · 32% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
D, E, FTrwg proteinprotein13732% helix, 35% strandO50335

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16010.600.7477empty
24390.570.7448empty
34330.560.7458empty

Interfaces

2 interfaces between chains.

  • D–E · 138 Ų buried · 7 hydrogen bonds · protein-protein
  • E–F · 84 Ų buried · 0 hydrogen bonds · protein-protein

Compared structures

  • 7Q1V · Arches protomer (trimer of TrwG/VirB8peri) structure from the fully-assembled R388 type… · the same entry in another collection · chain D against D, TM-score 1.00

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