Research workbench
Crystal structure of the ternary complex between the type 1 pilus proteins fimc, fimi and fima from E. COLI
Analyse Crystal structure of the ternary complex between the type 1 pilus proteins… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6SWH
- Type
- protein
- Length
- 961 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein fimc; Fimbrin-like protein fimi; Type-1 fimbrial protein, a chain
- UniProt
- P31697, P39264, P04128
- Pockets
- 10 · best druggability 0.85
Structure
x-ray diffraction · 5 distinct chains · 5% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D | Chaperone protein fimc | protein | 205 | 4% helix, 54% strand | P31697 |
| B | Fimbrin-like protein fimi | protein | 147 | 7% helix, 46% strand | P39264 |
| C | Type-1 fimbrial protein, a chain | protein | 112 | 4% helix, 48% strand | P04128 |
| E | Fimbrin-like protein fimi | protein | 150 | 3% helix, 49% strand | P39264 |
| F | Type-1 fimbrial protein, a chain | protein | 142 | 6% helix, 50% strand | P04128 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1122 | 0.85 | 0.86 | 83 | empty |
| 2 | 341 | 0.63 | 0.79 | 50 | empty |
| 3 | 107 | 0.58 | 0.86 | 26 | PEG |
| 4 | 211 | 0.52 | 0.77 | 21 | empty |
| 5 | 195 | 0.47 | 0.75 | 38 | empty |
Interfaces
10 interfaces between chains.
- A–B · 1988 Ų buried · 41 hydrogen bonds · protein-protein
- D–E · 1878 Ų buried · 40 hydrogen bonds · protein-protein
- E–F · 1314 Ų buried · 37 hydrogen bonds · protein-protein
- B–C · 1087 Ų buried · 33 hydrogen bonds · protein-protein
- D–F · 377 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 6SWH · Crystal structure of the ternary complex between the type 1 pilus proteins FimC, FimI and… · the same entry in another collection · chain C against C, TM-score 1.00
- P31697 · AlphaFold monomer V2.0 prediction for chaperone protein fimc (P31697) · a predicted model of the same protein · chain D against A, TM-score 0.98
- P04128 · AlphaFold monomer V2.0 prediction for type-1 fimbrial protein, a chain (P04128) · a predicted model of the same protein · chain F against A, TM-score 0.98
- P39264 · AlphaFold monomer V2.0 prediction for fimbrin-like protein fimi (P39264) · a predicted model of the same protein · chain E against A, TM-score 0.89
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 P39264
- Every structure of UniProt P04128
- Elsewhere: RCSB PDB 6SWH · PDBe 6SWH · UniProt P31697 · UniProt P39264 · UniProt P04128
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.