Research workbench
F9 pilus adhesin FmlH lectin domain from E. coli UTI89 co-crystallized with 8-hydroxyquinoline beta-galactoside
Analyse F9 pilus adhesin FmlH lectin domain from E. coli UTI89 co-crystallized with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ARO
- Type
- protein
- Length
- 310 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.2
- Source
- Escherichia coli
- Molecule
- F9 pilus adhesin FmlH
- UniProt
- Q1RBS0
- Ligands
- BS7, SO4
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · resolution 1.2 · 2 distinct chains · 4% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | F9 pilus adhesin FmlH | protein | 157 | 4% helix, 48% strand | Q1RBS0 |
| B | F9 pilus adhesin FmlH | protein | 153 | 3% helix, 48% strand | Q1RBS0 |
Ligands and binding sites
- BS7 · 8-hydroxyquinoline beta-galactopyranoside · sugar · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 266 | 0.52 | 0.76 | 31 | empty |
Interfaces
1 interface between chains.
- A–B · 518 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6ARO · F9 pilus adhesin fmlh lectin domain from E. COLI UTI89 co-crystallized with… · 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 Q1RBS0
- Elsewhere: RCSB PDB 6ARO · PDBe 6ARO · UniProt Q1RBS0
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