MolNFT v1 · #107821 · protein
Structure of the A_EQUINE_RICHMOND_07 H3 haemagglutinin in complex with 3SLN
4UO1 · Hemagglutinin: “Structure of the A_EQUINE_RICHMOND_07 H3 haemagglutinin in complex with 3SLN”. X-ray diffraction, 6 ligands (NAG, MAN, BMA), 19 pockets (best druggability 0.85). MolNFT v1 #107821 on GenesisL1: 3D structure, binding…
- PDB
- 4UO1
- Type
- protein
- Length
- 1,484 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemagglutinin
- UniProt
- C3TUR9
- Ligands
- NAG, MAN, BMA, FUC, GAL, SIA
- Pockets
- 19 · best druggability 0.85
Structure
x-ray diffraction · 5 distinct chains · 20% helix, 32% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemagglutinin | protein | 325 | 10% helix, 38% strand | C3TUR9 |
| B, F | Hemagglutinin | protein | 172 | 51% helix, 16% strand | C3TUR9 |
| C | Hemagglutinin | protein | 319 | 9% helix, 38% strand | C3TUR9 |
| D | Hemagglutinin | protein | 171 | 47% helix, 14% strand | C3TUR9 |
| E | Hemagglutinin | protein | 325 | 10% helix, 38% strand | C3TUR9 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 32 copies · chains A, E, B, C, F, D
- MAN · alpha-D-mannopyranose · sugar · 6 copies · chains C
- BMA · beta-D-mannopyranose · sugar · 5 copies · chains E, A, C
- FUC · alpha-L-fucopyranose · sugar · 5 copies · chains A, B, F, D
- GAL · beta-D-galactopyranose · sugar · 3 copies · chains A, C, E
- SIA · N-acetyl-alpha-neuraminic acid · sugar · 3 copies · chains A, C, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
19 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 901 | 0.85 | 0.87 | 118 | empty |
| 2 | 279 | 0.85 | 0.95 | 31 | empty |
| 3 | 1157 | 0.75 | 0.78 | 110 | empty |
| 4 | 834 | 0.73 | 0.78 | 74 | empty |
| 5 | 354 | 0.73 | 0.84 | 51 | empty |
Interfaces
15 interfaces between chains.
- E–F · 3161 Ų buried · 45 hydrogen bonds · protein-protein
- A–B · 3040 Ų buried · 43 hydrogen bonds · protein-protein
- C–D · 3008 Ų buried · 43 hydrogen bonds · protein-protein
- D–F · 1495 Ų buried · 16 hydrogen bonds · protein-protein
- B–F · 1489 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 glycan, 15 disulfide (N-glycosylation, disulfide).
Compared structures
- 4UO1 · Structure of the A_Equine_Richmond_07 H3 haemagglutinin in complex with 3SLN · 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 C3TUR9
- Elsewhere: RCSB PDB 4UO1 · PDBe 4UO1 · UniProt C3TUR9
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