Research workbench
Structure of the F4 fimbrial chaperone faee
Analyse Structure of the F4 fimbrial chaperone faee in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F6L
- Type
- protein
- Length
- 408 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chaperone protein faee
- UniProt
- P25401
- Pockets
- 3 · best druggability 0.56
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 49% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Chaperone protein faee | protein | 204 | 3% helix, 49% strand | P25401 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 96 | 0.56 | 0.85 | 17 | empty |
| 2 | 108 | 0.53 | 0.83 | 20 | empty |
| 3 | 188 | 0.49 | 0.76 | 39 | empty |
Interfaces
1 interface between chains.
- A–B · 596 Ų buried · 13 hydrogen bonds · protein-protein
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 P25401
- Elsewhere: RCSB PDB 3F6L · PDBe 3F6L · UniProt P25401
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