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Cryo-EM structure of the type 1 pilus rod

Analyse Cryo-EM structure of the type 1 pilus rod in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6C53
Type
protein
Length
1,716 residues
Chains
11
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Type-1 fimbrial protein, a chain
UniProt
P04128
Pockets
20 · best druggability 0.75

Structure

electron microscopy · 1 distinct chain · 3% helix, 41% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, I, J, KType-1 fimbrial protein, a chainprotein1563% helix, 41% strandP04128

Pockets

20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18940.750.7988empty
29220.720.77131empty
34460.630.7762empty
43440.630.7948empty
53230.620.7944empty

Interfaces

34 interfaces between chains.

  • B–D · 1622 Ų buried · 44 hydrogen bonds · protein-protein
  • G–I · 1621 Ų buried · 44 hydrogen bonds · protein-protein
  • A–B · 1620 Ų buried · 44 hydrogen bonds · protein-protein
  • F–H · 1618 Ų buried · 44 hydrogen bonds · protein-protein
  • H–J · 1617 Ų buried · 44 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 11 disulfide (disulfide).

Compared structures

  • 6C53 · Cryo-EM structure of the Type 1 pilus rod · the same entry in another collection · chain E against E, TM-score 1.00
  • P04128 · AlphaFold monomer V2.0 prediction for type-1 fimbrial protein, a chain (P04128) · a predicted model of the same protein · chain I against A, TM-score 0.95

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