MolNFT v1 · #147061 · protein
Handover mechanism of the growing pilus by the bacterial outer membrane usher fimd
6E15 · Chaperone protein fimc: “Handover mechanism of the growing pilus by the bacterial outer membrane usher fimd”. Electron microscopy, 20 pockets (best druggability 0.85). MolNFT v1 #147061 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6E15
- Type
- protein
- Length
- 1,554 residues
- Chains
- 5
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein fimc; Fimbrial biogenesis outer membrane usher protein; Protein fimf…
- UniProt
- P31697, A0A0F3W955, P08189, P08190, P08191
- Pockets
- 20 · best druggability 0.85
Structure
electron microscopy · 5 distinct chains · 3% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | Chaperone protein fimc | protein | 199 | 2% helix, 48% strand | P31697 |
| D | Fimbrial biogenesis outer membrane usher protein | protein | 778 | 5% helix, 53% strand | A0A0F3W955 |
| F | Protein fimf | protein | 154 | 5% helix, 35% strand | P08189 |
| G | Protein fimg | protein | 144 | 0% helix, 46% strand | P08190 |
| H | Type 1 fimbrin D-mannose specific adhesin | protein | 279 | 2% helix, 47% strand | P08191 |
Pockets
20 pockets found on a 1 Å grid, 18 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 719 | 0.85 | 0.89 | 110 | empty |
| 2 | 412 | 0.84 | 0.92 | 74 | empty |
| 3 | 479 | 0.83 | 0.90 | 105 | empty |
| 4 | 347 | 0.79 | 0.89 | 66 | empty |
| 5 | 324 | 0.79 | 0.89 | 55 | empty |
Interfaces
8 interfaces between chains.
- F–G · 1351 Ų buried · 33 hydrogen bonds · protein-protein
- D–G · 1281 Ų buried · 8 hydrogen bonds · protein-protein
- C–F · 1257 Ų buried · 22 hydrogen bonds · protein-protein
- G–H · 1209 Ų buried · 24 hydrogen bonds · protein-protein
- C–D · 680 Ų buried · 8 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 6E15 · Handover mechanism of the growing pilus by the bacterial outer membrane usher FimD · the same entry in another collection · chain H against H, TM-score 1.00
- P08191 · AlphaFold monomer V2.0 prediction for type 1 fimbrin D-mannose specific adhesin (P08191) · a predicted model of the same protein · chain H against A, TM-score 0.96
- P31697 · AlphaFold monomer V2.0 prediction for chaperone protein fimc (P31697) · a predicted model of the same protein · chain C against A, TM-score 0.95
- P08190 · AlphaFold monomer V2.0 prediction for protein fimg (P08190) · a predicted model of the same protein · chain G against A, TM-score 0.88
- P08189 · AlphaFold monomer V2.0 prediction for protein fimf (P08189) · a predicted model of the same protein · chain F against A, TM-score 0.81
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 P31697
- Every structure of UniProt A0A0F3W955
- Every structure of UniProt P08189
- Every structure of UniProt P08190
- Every structure of UniProt P08191
- Elsewhere: RCSB PDB 6E15 · PDBe 6E15 · UniProt P31697 · UniProt A0A0F3W955 · UniProt P08189 · UniProt P08190 · UniProt P08191
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.