Research workbench
F17a-G lectin domain with bound GlcNAc(beta1-3)Gal
Analyse F17a-G lectin domain with bound GlcNAc(beta1-3)Gal in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F6J
- Type
- protein
- Length
- 167 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.75
- Source
- Escherichia coli
- Molecule
- F17a-G
- UniProt
- Q99003
- Ligands
- MBG, NAG
Structure
x-ray diffraction · resolution 1.75 · 1 distinct chain · 2% helix, 59% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | F17a-G | protein | 167 | 2% helix, 59% strand | Q99003 |
Ligands and binding sites
- MBG · methyl beta-D-galactopyranoside · sugar · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 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
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 3F6J · PDBe 3F6J · UniProt Q99003
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