MolNFT v1 · #24580 · protein
Crystal structure of the dengue type 3 virus envelope protein
1UZG · Major envelope protein E: “Crystal structure of the dengue type 3 virus envelope protein”. X-ray diffraction, 4 ligands (NAG, FUL, BMA), 9 pockets (best druggability 0.63). MolNFT v1 #24580 on GenesisL1: 3D structure, binding sites…
- PDB
- 1UZG
- Type
- protein
- Length
- 784 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Major envelope protein E
- UniProt
- P27915
- Ligands
- NAG, FUL, BMA, MAN
- Pockets
- 9 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 5% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Major envelope protein E | protein | 392 | 5% helix, 45% strand | P27915 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A, B
- FUL · beta-L-fucopyranose · sugar · 3 copies · chains A, B
- BMA · beta-D-mannopyranose · sugar · 3 copies
- MAN · alpha-D-mannopyranose · sugar
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 390 | 0.63 | 0.78 | 45 | empty |
| 2 | 346 | 0.60 | 0.77 | 46 | empty |
| 3 | 108 | 0.54 | 0.83 | 28 | empty |
| 4 | 194 | 0.46 | 0.74 | 31 | empty |
| 5 | 172 | 0.45 | 0.75 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 1695 Ų buried · 19 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 12 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
- 1UZG · Crystal structure of the dengue type 3 virus envelope protein · 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 P27915
- Elsewhere: RCSB PDB 1UZG · PDBe 1UZG · UniProt P27915
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