Research workbench
Low resolution architecture of curli complex
Analyse Low 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
- 6LQJ
- Type
- protein
- Length
- 2,214 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 0.87
Structure
electron microscopy · 2 distinct chains · 23% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I | Curli production ASSEMBLY/TRANSPORT component csgg | protein | 206 | 21% helix, 44% strand | P0AEA2 |
| a, b, c, d, e, f, g, h, i | Curli production ASSEMBLY/TRANSPORT component csgf | protein | 40 | 30% helix, 0% strand | P0AE98 |
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1018 | 0.87 | 0.88 | 232 | empty |
| 2 | 64 | 0.75 | 1.00 | 21 | empty |
| 3 | 63 | 0.74 | 0.99 | 21 | empty |
| 4 | 64 | 0.74 | 0.99 | 19 | empty |
| 5 | 60 | 0.74 | 0.99 | 20 | empty |
Interfaces
45 interfaces between chains.
- E–H · 2416 Ų buried · 52 hydrogen bonds · protein-protein
- A–B · 2404 Ų buried · 49 hydrogen bonds · protein-protein
- B–E · 2398 Ų buried · 50 hydrogen bonds · protein-protein
- F–H · 2385 Ų buried · 51 hydrogen bonds · protein-protein
- C–G · 2384 Ų buried · 49 hydrogen bonds · protein-protein
Compared structures
- 6LQJ · Low resolution architecture of curli complex · the same entry in another collection · chain b against b, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P0AEA2
- Every structure of UniProt P0AE98
- Elsewhere: RCSB PDB 6LQJ · PDBe 6LQJ · UniProt P0AEA2 · UniProt P0AE98
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