Research workbench
Structural and functional characterization of neuraminidase-like molecule N10 derived from bat influenza a virus
Analyse Structural and functional characterization of neuraminidase-like molecule N10… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4FVK
- Type
- protein
- Length
- 734 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Neuraminidase
- EC
- 3.2.1.18
- UniProt
- H6QM75
- Ligands
- NAG, ZN, CA
- Pockets
- 10 · best druggability 0.61
Structure
x-ray diffraction · 1 distinct chain · 1% helix, 47% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Neuraminidase (EC 3.2.1.18) | protein | 367 | 1% helix, 47% strand | H6QM75 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, B
- ZN · Zinc ion · metal · 6 copies · chains A, B
- CA · Calcium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 257 | 0.61 | 0.80 | 44 | empty |
| 2 | 169 | 0.46 | 0.76 | 34 | empty |
| 3 | 66 | 0.44 | 0.82 | 18 | empty |
| 4 | 111 | 0.41 | 0.77 | 23 | empty |
| 5 | 134 | 0.41 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 238 Ų buried · 1 hydrogen bond · protein-protein
Modifications
Observed in the structure: 14 disulfide, 4 glycan (disulfide, N-glycosylation).
Compared structures
- 4FVK · Structural and functional characterization of neuraminidase-like molecule N10 derived… · 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 H6QM75
- Elsewhere: RCSB PDB 4FVK · PDBe 4FVK · UniProt H6QM75
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