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Architecture of curli complex

Analyse 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
7BRM
Type
protein
Length
2,619 residues
Chains
18
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Curli production ASSEMBLY/TRANSPORT protein csgg; Csgf
UniProt
A0A4V3YU48
Pockets
20 · best druggability 0.81

Structure

electron microscopy · 2 distinct chains · 26% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, ICurli production ASSEMBLY/TRANSPORT protein csggprotein25725% helix, 35% strandA0A4V3YU48
a, b, c, d, e, f, g, h, iCsgfprotein3435% helix, 0% strand—

Pockets

20 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19740.810.83110empty
211410.790.81111empty
33270.690.8345empty
43670.680.8144empty
53460.660.8141empty

Interfaces

54 interfaces between chains.

  • G–I · 3138 Ų buried · 50 hydrogen bonds · protein-protein
  • A–B · 3137 Ų buried · 48 hydrogen bonds · protein-protein
  • C–D · 3133 Ų buried · 47 hydrogen bonds · protein-protein
  • E–H · 3123 Ų buried · 45 hydrogen bonds · protein-protein
  • A–I · 3122 Ų buried · 46 hydrogen bonds · protein-protein

Compared structures

  • 7BRM · Architecture of curli complex · the same entry in another collection · chain A against A, TM-score 1.00

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