Research workbench
Crystal structure of H7 hemagglutinin mutant H7-svtq ( A138S, P221T, L226Q) with 6'SLN
Analyse Crystal structure of H7 hemagglutinin mutant H7-svtq ( A138S, P221T, L226Q)… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6IDB
- Type
- protein
- Length
- 489 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemagglutinin HA1 chain; Hemagglutinin HA2 chain
- UniProt
- R4NN21
- Ligands
- NAG, GAL, SIA
- Pockets
- 4 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 25% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemagglutinin HA1 chain | protein | 317 | 9% helix, 41% strand | R4NN21 |
| B | Hemagglutinin HA2 chain | protein | 172 | 56% helix, 12% strand | R4NN21 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B
- GAL · beta-D-galactopyranose · sugar · chains A
- SIA · N-acetyl-alpha-neuraminic acid · sugar · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 247 | 0.64 | 0.82 | 25 | empty |
| 2 | 98 | 0.45 | 0.80 | 22 | empty |
| 3 | 53 | 0.39 | 0.81 | 15 | empty |
| 4 | 50 | 0.27 | 0.74 | 11 | empty |
Interfaces
1 interface between chains.
- A–B · 3237 Ų buried · 43 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 2 glycan (disulfide, N-glycosylation).
Compared structures
- 6IDB · Crystal structure of H7 hemagglutinin mutant H7-SVTQ ( A138S, P221T, L226Q) with 6'SLN · 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 R4NN21
- Elsewhere: RCSB PDB 6IDB · PDBe 6IDB · UniProt R4NN21
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