Research workbench
Structure of a chaperone-usher pilus reveals the molecular basis of rod uncoilin
Analyse Structure of a chaperone-usher pilus reveals the molecular basis of rod uncoilin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FLU
- Type
- protein
- Length
- 2,119 residues
- Chains
- 13
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pap fimbrial major pilin protein
- UniProt
- P04127
- Pockets
- 20 · best druggability 0.73
Structure
electron microscopy · 1 distinct chain · 9% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K, L, M | Pap fimbrial major pilin protein | protein | 163 | 9% helix, 44% strand | P04127 |
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 826 | 0.73 | 0.78 | 68 | empty |
| 2 | 836 | 0.73 | 0.78 | 65 | empty |
| 3 | 765 | 0.73 | 0.78 | 75 | empty |
| 4 | 802 | 0.72 | 0.78 | 73 | empty |
| 5 | 842 | 0.71 | 0.76 | 80 | empty |
Interfaces
50 interfaces between chains.
- F–G · 1583 Ų buried · 37 hydrogen bonds · protein-protein
- D–E · 1582 Ų buried · 37 hydrogen bonds · protein-protein
- J–K · 1581 Ų buried · 37 hydrogen bonds · protein-protein
- E–F · 1579 Ų buried · 37 hydrogen bonds · protein-protein
- A–H · 1577 Ų buried · 37 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 13 disulfide (disulfide).
Compared structures
- 5FLU · Structure of a Chaperone-Usher pilus reveals the molecular basis of rod uncoilin · the same entry in another collection · chain M against M, 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 P04127
- Elsewhere: RCSB PDB 5FLU · PDBe 5FLU · UniProt P04127
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