MolNFT v1 · #14987 · protein
BHA/LSTA
1MQM · Hemagglutinin HA1 chain: “BHA/LSTA”. X-ray diffraction, 5 ligands (NAG, BMA, MAN), 15 pockets (best druggability 0.87). MolNFT v1 #14987 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 1MQM
- Type
- protein
- Length
- 1,470 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemagglutinin HA1 chain; Hemagglutinin HA2 chain
- UniProt
- P03442
- Ligands
- NAG, BMA, MAN, GAL, SIA
- Pockets
- 15 · best druggability 0.87
Structure
x-ray diffraction · 2 distinct chains · 24% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, D, G | Hemagglutinin HA1 chain | protein | 318 | 10% helix, 38% strand | P03442 |
| B, E, H | Hemagglutinin HA2 chain | protein | 172 | 52% helix, 15% strand | P03442 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 21 copies · chains A, G, B, D, E, H
- BMA · beta-D-mannopyranose · sugar · 3 copies · chains G, A, D
- MAN · alpha-D-mannopyranose · sugar · 3 copies
- GAL · beta-D-galactopyranose · sugar · 3 copies · chains A, D, G
- SIA · N-acetyl-alpha-neuraminic acid · sugar · 3 copies · chains A, D, G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
15 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1154 | 0.87 | 0.88 | 132 | empty |
| 2 | 512 | 0.83 | 0.89 | 46 | empty |
| 3 | 279 | 0.76 | 0.88 | 55 | empty |
| 4 | 290 | 0.74 | 0.87 | 28 | empty |
| 5 | 278 | 0.73 | 0.87 | 47 | empty |
Interfaces
15 interfaces between chains.
- D–E · 3021 Ų buried · 49 hydrogen bonds · protein-protein
- G–H · 3010 Ų buried · 49 hydrogen bonds · protein-protein
- A–B · 2936 Ų buried · 44 hydrogen bonds · protein-protein
- E–H · 1528 Ų buried · 29 hydrogen bonds · protein-protein
- B–E · 1494 Ų buried · 24 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 18 disulfide, 14 glycan (disulfide, N-glycosylation).
Compared structures
- 1MQM · BHA/LSTa · 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 P03442
- Elsewhere: RCSB PDB 1MQM · PDBe 1MQM · UniProt P03442
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