Research workbench
Crystal structure of fungal lectin : six-bladed beta-propeller fold and novel fucose recognition mode for aleuria aurantia lectin
Analyse Crystal structure of fungal lectin : six-bladed beta-propeller fold and novel… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OFZ
- Type
- protein
- Length
- 624 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fucose-specific lectin
- UniProt
- P18891
- Ligands
- FUL, FUC
- Pockets
- 4 · best druggability 0.78
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 54% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Fucose-specific lectin | protein | 312 | 3% helix, 54% strand | P18891 |
Ligands and binding sites
- FUL · beta-L-fucopyranose · sugar · 8 copies · chains A, B
- FUC · alpha-L-fucopyranose · sugar · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 854 | 0.78 | 0.81 | 113 | empty |
| 2 | 481 | 0.75 | 0.83 | 52 | empty |
| 3 | 64 | 0.32 | 0.75 | 16 | FUL, FUC |
| 4 | 58 | 0.31 | 0.76 | 17 | FUC, FUL |
Interfaces
1 interface between chains.
- A–B · 1011 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 1OFZ · Crystal structure of fungal lectin : six-bladed beta-propeller fold and novel fucose… · the same entry in another collection · chain A against A, TM-score 1.00
- P18891 · AlphaFold monomer V2.0 prediction for fucose-specific lectin (P18891) · a predicted model of the same protein · 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 P18891
- Elsewhere: RCSB PDB 1OFZ · PDBe 1OFZ · UniProt P18891
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