MolNFT v1 · #170760 · protein
In-situ structure of the trimeric hef from influenza C by flexible fitting into a cryo-et MAP.
6YI5: “In-situ structure of the trimeric hef from influenza C by flexible fitting into a cryo-et MAP.”. Electron microscopy, 3 ligands (NAG, BMA, NDG). MolNFT v1 #170760 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6YI5
- Type
- protein
- Length
- 1,767 residues
- Chains
- 6
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- P07975
- Ligands
- NAG, BMA, NDG
Structure
electron microscopy · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E, C | — | protein | 427 | — | P07975 |
| B, F, D | — | protein | 162 | — | P07975 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 15 copies · chains A, B, C, E, F, D
- BMA · beta-D-mannopyranose · sugar · 9 copies · chains B, D
- NDG · 2-acetamido-2-deoxy-alpha-D-glucopyranose · sugar · 3 copies · chains B, C, F, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6YI5 · In-situ structure of the trimeric HEF from influenza C by flexible fitting into a cryo-ET… · 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 P07975
- Elsewhere: RCSB PDB 6YI5 · PDBe 6YI5 · UniProt P07975
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.