MolNFT v1 · #108670 · protein
Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins
4WE7 · Hemagglutinin HA1 chain: “Structure and receptor binding preferences of recombinant human A(H3N2) virus hemagglutinins”. X-ray diffraction, 1 ligand (NAG), 3 pockets (best druggability 0.69). MolNFT v1 #108670 on GenesisL1: 3D…
- PDB
- 4WE7
- Type
- protein
- Length
- 1,088 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemagglutinin HA1 chain
- UniProt
- U3N7S5
- Ligands
- NAG
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 11% helix, 38% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Hemagglutinin HA1 chain | protein | 272 | 11% helix, 38% strand | U3N7S5 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 14 copies · chains A, B, C, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 585 | 0.69 | 0.78 | 51 | empty |
| 2 | 596 | 0.69 | 0.78 | 48 | empty |
| 3 | 193 | 0.50 | 0.76 | 38 | empty |
Interfaces
5 interfaces between chains.
- A–D · 408 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 406 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 396 Ų buried · 0 hydrogen bonds · protein-protein
- A–B · 395 Ų buried · 1 hydrogen bond · protein-protein
- B–D · 132 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 16 disulfide, 14 glycan (disulfide, N-glycosylation).
Compared structures
- 4WE7 · Structure and receptor binding preferences of recombinant human A(H3N2) virus… · the same entry in another collection · chain C against C, 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 U3N7S5
- Elsewhere: RCSB PDB 4WE7 · PDBe 4WE7 · UniProt U3N7S5
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