Research workbench
BambL complexed with Htype2 tetrasaccharide
Analyse BambL complexed with Htype2 tetrasaccharide in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3ZZV
- Type
- protein
- Length
- 261 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.68
- Source
- BURKHOLDERIA AMBIFARIA
- Molecule
- Bambl lectin
- UniProt
- Q0B4G1
- Ligands
- FUC, NAG, GAL
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · resolution 1.68 · 1 distinct chain · 0% helix, 69% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | Bambl lectin | protein | 87 | 0% helix, 69% strand | Q0B4G1 |
Ligands and binding sites
- FUC · alpha-L-fucopyranose · sugar · 6 copies · chains A, B, C
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, B, C
- GAL · beta-D-galactopyranose · sugar · 5 copies · chains A, B, C
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 | 526 | 0.73 | 0.82 | 48 | empty |
Interfaces
3 interfaces between chains.
- A–B · 713 Ų buried · 8 hydrogen bonds · protein-protein
- A–C · 697 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 684 Ų buried · 8 hydrogen bonds · protein-protein
Compared structures
- 3ZZV · Bambl complexed with HTYPE2 tetrasaccharide · 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 Q0B4G1
- Elsewhere: RCSB PDB 3ZZV · PDBe 3ZZV · UniProt Q0B4G1
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