Research workbench
Mistletoe lectin I from viscum album
Analyse Mistletoe lectin I from viscum album in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ONK
- Type
- protein
- Length
- 512 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Beta-galactoside specific lectin I a chain; Galactose specific lectin I B chain
- EC
- 3.2.2.22
- UniProt
- P81446, P81830
- Ligands
- NAG, AZI, PO4
- Pockets
- 5 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Beta-galactoside specific lectin I a chain (EC 3.2.2.22) | protein | 249 | 38% helix, 28% strand | P81446 |
| B | Galactose specific lectin I B chain | protein | 263 | 11% helix, 37% strand | P81830 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
- AZI · Azide ion · ion · 9 copies · chains A, B
- PO4 · Phosphate ion · ion · chains A
- GOL · Glycerol · additive · 8 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 200 | 0.77 | 0.92 | 38 | AZI |
| 2 | 274 | 0.55 | 0.76 | 35 | AZI, GOL |
| 3 | 131 | 0.47 | 0.78 | 26 | empty |
| 4 | 142 | 0.47 | 0.78 | 25 | empty |
| 5 | 87 | 0.36 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1570 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide, 2 glycan (disulfide, N-glycosylation).
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 P81446
- Every structure of UniProt P81830
- Elsewhere: RCSB PDB 1ONK · PDBe 1ONK · UniProt P81446 · UniProt P81830
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