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Structure of the curli secretion-assembly complex CSGG:CSGF

Analyse Structure of the curli secretion-assembly complex CSGG:CSGF in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6SI7
Type
protein
Length
2,502 residues
Chains
18
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Curli production ASSEMBLY/TRANSPORT component csgf; Curli production ASSEMBLY/TRANSPORT…
UniProt
P0AE98, P0AEA2
Pockets
20 · best druggability 0.80

Structure

electron microscopy · 2 distinct chains · 24% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, G, H, ICurli production ASSEMBLY/TRANSPORT component csgfprotein3537% helix, 0% strandP0AE98
P, J, K, L, M, N, O, Q, RCurli production ASSEMBLY/TRANSPORT component csggprotein24322% helix, 36% strandP0AEA2

Pockets

20 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
16880.800.8596empty
27910.680.7572empty
31650.630.8525empty
41870.630.8428empty
51600.630.8530empty

Interfaces

45 interfaces between chains.

  • N–O · 3030 Ų buried · 62 hydrogen bonds · protein-protein
  • P–J · 3029 Ų buried · 62 hydrogen bonds · protein-protein
  • L–M · 3027 Ų buried · 62 hydrogen bonds · protein-protein
  • P–R · 3026 Ų buried · 62 hydrogen bonds · protein-protein
  • M–N · 3026 Ų buried · 62 hydrogen bonds · protein-protein

Compared structures

  • 6SI7 · Structure of the curli secretion-assembly complex CsgG:CsgF · the same entry in another collection · chain M against M, TM-score 1.00

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