MolNFT v1 · #165437 · protein
Crystal structure of the haemagglutinin from a H10N7 seal influenza virus isolated in germany in complex with avian receptor analogue, 3'-sln
6TVD: “Crystal structure of the haemagglutinin from a H10N7 seal influenza virus isolated in germany in complex with…”. X-ray diffraction, 4 ligands (NAG, GAL, SIA). MolNFT v1 #165437 on GenesisL1: 3D structure, binding sites and pockets…
- PDB
- 6TVD
- Type
- protein
- Length
- 2,940 residues
- Chains
- 12
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A0A7HR51
- Ligands
- NAG, GAL, SIA, CA
Structure
x-ray diffraction · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 320 | — | A0A0A7HR51 |
| B, D, F, H, J, L | — | protein | 172 | — | A0A0A7HR51 |
| C, E, I, K | — | protein | 318 | — | A0A0A7HR51 |
| G | — | protein | 316 | — | A0A0A7HR51 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 24 copies · chains D, K, C, E, F, A, H, G, I, J, L, B
- GAL · beta-D-galactopyranose · sugar · 6 copies · chains A, C, E, G, I, K
- SIA · N-acetyl-alpha-neuraminic acid · sugar · 6 copies · chains A, C, E, G, I, K
- CA · Calcium ion · metal · 3 copies · chains A, B, H, G, J, D, K, L
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6TVD · Crystal structure of the haemagglutinin from a H10N7 seal influenza virus isolated in… · 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 A0A0A7HR51
- Elsewhere: RCSB PDB 6TVD · PDBe 6TVD · UniProt A0A0A7HR51
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.