Research workbench
Lectin uea-II complexed with fucosyllactose and fucosylgalactose
Analyse Lectin uea-II complexed with fucosyllactose and fucosylgalactose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QOT
- Type
- protein
- Length
- 942 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Chitin binding lectin, uea-II
- Ligands
- GAL, FUC, NAG, GLC, MN, CA
- Pockets
- 1 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Chitin binding lectin, uea-II | protein | 234 | 7% helix, 45% strand | — |
| B, C, D | Chitin binding lectin, uea-II | protein | 236 | 7% helix, 44% strand | — |
Ligands and binding sites
- GAL · beta-D-galactopyranose · sugar · 4 copies · chains A, B, C, D
- FUC · alpha-L-fucopyranose · sugar · 4 copies · chains A, B, C, D
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A, B, C, D
- GLC · alpha-D-glucopyranose · sugar · chains C
- MN · Manganese (II) ion · metal · 4 copies · chains A, B, C, D
- CA · Calcium ion · metal · 4 copies · chains A, B, C, D
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 | 933 | 0.81 | 0.83 | 96 | empty |
Interfaces
6 interfaces between chains.
- A–B · 988 Ų buried · 7 hydrogen bonds · protein-protein
- C–D · 981 Ų buried · 7 hydrogen bonds · protein-protein
- B–D · 761 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 757 Ų buried · 6 hydrogen bonds · protein-protein
- A–D · 74 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 glycan, 2 disulfide (O-glycosylation, disulfide).
Compared structures
- 1QOT · lectin UEA-II complexed with fucosyllactose and fucosylgalactose · 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
- Elsewhere: RCSB PDB 1QOT · PDBe 1QOT
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