MolNFT v1 · #107823 · protein
Structure of the A_EQUINE_RICHMOND_07 H3 haemagglutinin mutant SER30THR
4UO3 · H3 haemagglutinin HA1 chain: “Structure of the A_EQUINE_RICHMOND_07 H3 haemagglutinin mutant SER30THR”. X-ray diffraction, 4 ligands (NAG, MAN, BMA), 14 pockets (best druggability 0.86). MolNFT v1 #107823 on GenesisL1: 3D structure…
- PDB
- 4UO3
- Type
- protein
- Length
- 1,481 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- H3 haemagglutinin HA1 chain; H3 haemagglutinin HA2 chain
- UniProt
- C3TUR9
- Ligands
- NAG, MAN, BMA, FUC
- Pockets
- 14 · best druggability 0.86
Structure
x-ray diffraction · 5 distinct chains · 21% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | H3 haemagglutinin HA1 chain | protein | 323 | 10% helix, 39% strand | C3TUR9 |
| B, D | H3 haemagglutinin HA2 chain | protein | 172 | 55% helix, 15% strand | C3TUR9 |
| C | H3 haemagglutinin HA1 chain | protein | 320 | 10% helix, 39% strand | C3TUR9 |
| E | H3 haemagglutinin HA1 chain | protein | 323 | 10% helix, 39% strand | C3TUR9 |
| F | H3 haemagglutinin HA2 chain | protein | 171 | 54% helix, 15% strand | C3TUR9 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 22 copies · chains A, B, E, C, D, F
- MAN · alpha-D-mannopyranose · sugar · 8 copies · chains C, D
- BMA · beta-D-mannopyranose · sugar · 6 copies · chains E, A, C
- FUC · alpha-L-fucopyranose · sugar · 4 copies · chains A, B, D, F
- EDO · 1,2-ethanediol · additive · 3 copies · chains A, E, B, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
14 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1133 | 0.86 | 0.87 | 142 | EDO |
| 2 | 572 | 0.83 | 0.88 | 53 | empty |
| 3 | 732 | 0.77 | 0.82 | 74 | empty |
| 4 | 929 | 0.74 | 0.78 | 89 | empty |
| 5 | 690 | 0.72 | 0.79 | 62 | empty |
Interfaces
15 interfaces between chains.
- A–B · 3240 Ų buried · 50 hydrogen bonds · protein-protein
- E–F · 3193 Ų buried · 45 hydrogen bonds · protein-protein
- C–D · 3146 Ų buried · 45 hydrogen bonds · protein-protein
- D–F · 1449 Ų buried · 20 hydrogen bonds · protein-protein
- B–F · 1418 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 15 disulfide, 15 glycan (disulfide, N-glycosylation).
Compared structures
- 4UO3 · Structure of the A_Equine_Richmond_07 H3 haemagglutinin mutant Ser30Thr · the same entry in another collection · chain E against E, 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 4UO3 · PDBe 4UO3 · UniProt C3TUR9
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