Research workbench
F17-ag lectin domain from escherichia COLI in complex with a selenium carbohydrate derivative
Analyse F17-ag lectin domain from escherichia COLI in complex with a selenium… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1O9V
- Type
- protein
- Length
- 168 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- F17-ag lectin domain
- UniProt
- Q99003
- Ligands
- SNG
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 58% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | F17-ag lectin domain | protein | 168 | 2% helix, 58% strand | Q99003 |
Ligands and binding sites
- SNG · methyl 2-acetamido-2-deoxy-1-seleno-beta-D-glucopyranoside · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 1O9V · F17-aG lectin domain from Escherichia coli in complex with a selenium carbohydrate… · the same entry in another collection · chain A against A, TM-score 1.00
- Q99003 · AlphaFold monomer V2.0 prediction for F17A-G fimbrial adhesin (Q99003) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q99003
- Elsewhere: RCSB PDB 1O9V · PDBe 1O9V · UniProt Q99003
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