MolNFT v1 · #79268 · protein
Crystal structure of a fimbrial protein BF1861 [bacteroides fragilis nctc 9343] (BF1861) from bacteroides fragilis nctc 9343 at 1.90 a resolution
3SY6: “Crystal structure of a fimbrial protein BF1861 [bacteroides fragilis nctc 9343] (BF1861) from bacteroides…”. X-ray diffraction, 5 pockets (best druggability 0.35). MolNFT v1 #79268 on GenesisL1: 3D structure, binding sites and…
- PDB
- 3SY6
- Type
- protein
- Length
- 543 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fimbrial protein BF1861
- UniProt
- Q5LE92
- Pockets
- 5 · best druggability 0.35
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Fimbrial protein BF1861 | protein | 272 | 6% helix, 52% strand | Q5LE92 |
| B | Fimbrial protein BF1861 | protein | 271 | 6% helix, 52% strand | Q5LE92 |
Ligands and binding sites
- NHE · 2-[N-cyclohexylamino]ethane sulfonic acid · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 52 | 0.35 | 0.79 | 13 | empty |
| 2 | 75 | 0.33 | 0.75 | 21 | empty |
| 3 | 67 | 0.33 | 0.76 | 23 | empty |
| 4 | 92 | 0.31 | 0.73 | 23 | empty |
| 5 | 52 | 0.28 | 0.75 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1040 Ų buried · 20 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 modified (engineered).
Compared structures
- 3SY6 · Crystal structure of a fimbrial protein BF1861 [Bacteroides fragilis NCTC 9343] (BF1861)… · the same entry in another collection · chain A against A, 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 Q5LE92
- Elsewhere: RCSB PDB 3SY6 · PDBe 3SY6 · UniProt Q5LE92
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.