MolNFT v1 · #56632 · protein
Atomic resolution structural characterization of recognition of histo- blood group antigens by norwalk virus
2ZL6 · 58 kd capsid protein: “Atomic resolution structural characterization of recognition of histo- blood group antigens by norwalk virus”. X-ray diffraction, 5 ligands (GAL, BGC, NAG), 3 pockets (best druggability 0.75). MolNFT v1 #56632…
- PDB
- 2ZL6
- Type
- protein
- Length
- 573 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 58 kd capsid protein
- UniProt
- Q83884
- Ligands
- GAL, BGC, NAG, FUC, MG
- Pockets
- 3 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 9% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 58 kd capsid protein | protein | 286 | 9% helix, 32% strand | Q83884 |
| B | 58 kd capsid protein | protein | 287 | 9% helix, 33% strand | Q83884 |
Ligands and binding sites
- GAL · beta-D-galactopyranose · sugar · 2 copies · chains B
- BGC · beta-D-glucopyranose · sugar
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar
- FUC · alpha-L-fucopyranose · sugar · chains A, B
- MG · Magnesium ion · metal · 2 copies · chains A, B
- ACT · Acetate ion · additive · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 517 | 0.75 | 0.83 | 79 | ACT |
| 2 | 91 | 0.35 | 0.75 | 18 | empty |
| 3 | 86 | 0.33 | 0.74 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 1606 Ų buried · 22 hydrogen bonds · protein-protein
Compared structures
- 2ZL6 · Atomic resolution structural characterization of recognition of histo-blood group… · 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 Q83884
- Elsewhere: RCSB PDB 2ZL6 · PDBe 2ZL6 · UniProt Q83884
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