MolNFT v1 · #188653 · protein
Influenza neuraminidase N1-MI15-snap-174
7U2T · Influenza N1-MI15-snap-174: “Influenza neuraminidase N1-MI15-snap-174”. Electron microscopy, 1 ligand (NAG), 20 pockets (best druggability 0.64). MolNFT v1 #188653 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7U2T
- Type
- protein
- Length
- 1,336 residues
- Chains
- 4
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Influenza N1-MI15-snap-174
- Ligands
- NAG
- Pockets
- 20 · best druggability 0.64
Structure
electron microscopy · 1 distinct chain · 3% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Influenza N1-MI15-snap-174 | protein | 334 | 3% helix, 51% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 283 | 0.64 | 0.81 | 35 | empty |
| 2 | 259 | 0.64 | 0.82 | 34 | empty |
| 3 | 280 | 0.64 | 0.81 | 35 | empty |
| 4 | 269 | 0.64 | 0.81 | 35 | empty |
| 5 | 228 | 0.60 | 0.81 | 27 | empty |
Interfaces
4 interfaces between chains.
- B–C · 1316 Ų buried · 10 hydrogen bonds · protein-protein
- C–D · 1315 Ų buried · 10 hydrogen bonds · protein-protein
- A–D · 1315 Ų buried · 10 hydrogen bonds · protein-protein
- A–B · 1312 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 32 disulfide, 8 glycan (disulfide, N-glycosylation).
Compared structures
- 7U2T · Influenza Neuraminidase N1-MI15-sNAp-174 · 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
- Elsewhere: RCSB PDB 7U2T · PDBe 7U2T
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