Research workbench
Crystal structure of hemagglutinin
Analyse Crystal structure of hemagglutinin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3A5P
- Type
- protein
- Length
- 412 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Haemagglutinin I
- UniProt
- O60949
- Pockets
- 2 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 3% helix, 56% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Haemagglutinin I | protein | 103 | 3% helix, 56% strand | O60949 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 427 | 0.75 | 0.85 | 55 | empty |
| 2 | 106 | 0.40 | 0.76 | 18 | empty |
Interfaces
5 interfaces between chains.
- C–D · 904 Ų buried · 16 hydrogen bonds · protein-protein
- A–B · 894 Ų buried · 14 hydrogen bonds · protein-protein
- A–C · 346 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 326 Ų buried · 6 hydrogen bonds · protein-protein
- B–C · 61 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 3A5P · Crystal structure of hemagglutinin · 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 O60949
- Elsewhere: RCSB PDB 3A5P · PDBe 3A5P · UniProt O60949
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