Research workbench
Crystal structure of H7 hemagglutinin mutant H7-agtl ( V186G, P221T) from the influenza virus A/ANHUI/1/2013 (H7N9)
Analyse Crystal structure of H7 hemagglutinin mutant H7-agtl ( V186G, P221T) from the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6ICY
- Type
- protein
- Length
- 482 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
- Pockets
- 3 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 23% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Hemagglutinin HA1 chain | protein | 314 | 8% helix, 39% strand | R4NN21 |
| B | Hemagglutinin HA2 chain | protein | 168 | 52% helix, 12% strand | R4NN21 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 234 | 0.63 | 0.82 | 25 | empty |
| 2 | 114 | 0.46 | 0.79 | 22 | empty |
| 3 | 52 | 0.33 | 0.78 | 16 | empty |
Interfaces
1 interface between chains.
- A–B · 2994 Ų buried · 43 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
- 6ICY · Crystal structure of H7 hemagglutinin mutant H7-AGTL ( V186G, P221T) from the influenza… · 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 6ICY · PDBe 6ICY · UniProt R4NN21
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