Research workbench
Breaking down the wall: mutation of the tyrosine gate of the universal escherichia COLI fimbrial adhesin fimh
Analyse Breaking down the wall: mutation of the tyrosine gate of the universal… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5FWR
- Type
- protein
- Length
- 1,264 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fimh
- UniProt
- Q9S497
- Ligands
- 3X8
- Pockets
- 8 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 6% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Fimh | protein | 158 | 6% helix, 52% strand | Q9S497 |
Ligands and binding sites
- 3X8 · biphenyl-4-yl alpha-D-mannopyranoside · ligand · 8 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1066 | 0.80 | 0.82 | 123 | empty |
| 2 | 826 | 0.70 | 0.76 | 76 | empty |
| 3 | 386 | 0.58 | 0.75 | 52 | empty |
| 4 | 148 | 0.48 | 0.78 | 32 | empty |
| 5 | 149 | 0.44 | 0.75 | 29 | empty |
Interfaces
8 interfaces between chains.
- A–E · 621 Ų buried · 9 hydrogen bonds · protein-protein
- B–C · 547 Ų buried · 8 hydrogen bonds · protein-protein
- D–G · 543 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 355 Ų buried · 6 hydrogen bonds · protein-protein
- A–B · 353 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 5FWR · Breaking down the wall: mutation of the tyrosine gate of the universal Escherichia coli… · 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 Q9S497
- Elsewhere: RCSB PDB 5FWR · PDBe 5FWR · UniProt Q9S497
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