Research workbench
F9 pilus adhesin fmlh lectin domain from E. COLI UTI89 co-crystallized with O-methoxyphenyl beta-galactoside (ompg)
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
- 6ARN
- Type
- protein
- Length
- 302 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Putative fml fimbrial adhesin fmld
- UniProt
- Q1RBS0
- Ligands
- BQY, SO4
- Pockets
- 2 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 4% helix, 48% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Putative fml fimbrial adhesin fmld | protein | 150 | 5% helix, 48% strand | Q1RBS0 |
| B | Putative fml fimbrial adhesin fmld | protein | 152 | 2% helix, 49% strand | Q1RBS0 |
Ligands and binding sites
- BQY · 2-methoxyphenyl beta-D-galactopyranoside · ligand · 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
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 317 | 0.57 | 0.77 | 54 | empty |
| 2 | 74 | 0.35 | 0.76 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 515 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 6ARN · 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 6ARN · PDBe 6ARN · UniProt Q1RBS0
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