MolNFT v2 · #152281 · protein
Structure of Influenza Hemagglutinin ectodomain (A/duck/Alberta/35/76) in complex with FISW84 Fab Fragment
6HJP: “Structure of Influenza Hemagglutinin ectodomain (A/duck/Alberta/35/76) in complex with FISW84 Fab Fragment”. Electron microscopy at 3.3, 5 ligands (UPL, NAG, BMA). MolNFT v2 #152281 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6HJP
- Type
- protein
- Length
- 2,784 residues
- Chains
- 12
- Method
- electron microscopy
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 3.3
- Source
- Homo sapiens; Influenza A virus (strain A/Duck/Alberta/35/1976 H1N1)
- UniProt
- Q9WCE0, P26562
- Ligands
- UPL, NAG, BMA, MAN, FUC
Structure
electron microscopy · resolution 3.3 · 4 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C, E | — | protein | 324 | — | Q9WCE0 |
| B, D, F | — | protein | 174 | — | P26562 |
| G, I, K | — | protein | 216 | — | — |
| H, J, L | — | protein | 214 | — | — |
Ligands and binding sites
- UPL · Unknown branched fragment of phospholipid · ligand · 3 copies · chains B, D, F
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 30 copies · chains A, B, C, D, E, F
- BMA · beta-D-mannopyranose · sugar · 9 copies
- MAN · alpha-D-mannopyranose · sugar · 6 copies
- FUC · alpha-L-fucopyranose · sugar · 3 copies
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6HJP · Structure of influenza hemagglutinin ectodomain (A/DUCK/ALBERTA/35/76) in complex with… · 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 Q9WCE0
- Every structure of UniProt P26562
- Elsewhere: RCSB PDB 6HJP · PDBe 6HJP · UniProt Q9WCE0 · UniProt P26562
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