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High resolution architecture of curli complex

Analyse High resolution architecture of curli complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LQH
Type
protein
Length
2,160 residues
Chains
18
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Curli production ASSEMBLY/TRANSPORT component csgg; Curli production ASSEMBLY/TRANSPORT…
UniProt
P0AEA2, P0AE98
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 2 distinct chains · 23% helix, 39% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, ICurli production ASSEMBLY/TRANSPORT component csggprotein20621% helix, 44% strandP0AEA2
a, b, c, d, e, f, g, h, iCurli production ASSEMBLY/TRANSPORT component csgfprotein3432% helix, 6% strandP0AE98

Pockets

20 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17070.860.90174empty
2980.660.9131empty
36910.660.7572empty
4960.650.9028empty
5590.480.8517empty

Interfaces

45 interfaces between chains.

  • A–I · 2392 Ų buried · 46 hydrogen bonds · protein-protein
  • C–G · 2392 Ų buried · 48 hydrogen bonds · protein-protein
  • A–B · 2391 Ų buried · 48 hydrogen bonds · protein-protein
  • E–H · 2387 Ų buried · 47 hydrogen bonds · protein-protein
  • B–E · 2386 Ų buried · 46 hydrogen bonds · protein-protein

Compared structures

  • 6LQH · High resolution architecture of curli complex · the same entry in another collection · chain b against b, TM-score 1.00

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