Research workbench
Cryo-EM structure of the type 1 pilus rod
Analyse Cryo-EM structure of the type 1 pilus rod in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6C53
- Type
- protein
- Length
- 1,716 residues
- Chains
- 11
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Type-1 fimbrial protein, a chain
- UniProt
- P04128
- Pockets
- 20 · best druggability 0.75
Structure
electron microscopy · 1 distinct chain · 3% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H, I, J, K | Type-1 fimbrial protein, a chain | protein | 156 | 3% helix, 41% strand | P04128 |
Pockets
20 pockets found on a 1 Å grid, 14 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 894 | 0.75 | 0.79 | 88 | empty |
| 2 | 922 | 0.72 | 0.77 | 131 | empty |
| 3 | 446 | 0.63 | 0.77 | 62 | empty |
| 4 | 344 | 0.63 | 0.79 | 48 | empty |
| 5 | 323 | 0.62 | 0.79 | 44 | empty |
Interfaces
34 interfaces between chains.
- B–D · 1622 Ų buried · 44 hydrogen bonds · protein-protein
- G–I · 1621 Ų buried · 44 hydrogen bonds · protein-protein
- A–B · 1620 Ų buried · 44 hydrogen bonds · protein-protein
- F–H · 1618 Ų buried · 44 hydrogen bonds · protein-protein
- H–J · 1617 Ų buried · 44 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 11 disulfide (disulfide).
Compared structures
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 P04128
- Elsewhere: RCSB PDB 6C53 · PDBe 6C53 · UniProt P04128
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