Research workbench
Crystal structure of a complex formed between FLD194 Fab and transmissible mutant H5 haemagglutinin
Analyse Crystal structure of a complex formed between FLD194 Fab and transmissible… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5A3I
- Type
- protein
- Length
- 1,866 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Hemagglutinin; Anti-haemagglutinin HA1 Fab heavy chain; Anti-haemagglutinin HA1 Fab light…
- UniProt
- A5A5M5
- Ligands
- NAG
- Pockets
- 20 · best druggability 0.77
Structure
x-ray diffraction · 5 distinct chains · 22% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, E | Hemagglutinin | protein | 323 | 7% helix, 39% strand | A5A5M5 |
| B | Hemagglutinin | protein | 166 | 55% helix, 12% strand | A5A5M5 |
| C, G | Anti-haemagglutinin HA1 Fab heavy chain | protein | 226 | 8% helix, 47% strand | — |
| D, H | Anti-haemagglutinin HA1 Fab light chain | protein | 218 | 6% helix, 49% strand | — |
| F | Hemagglutinin | protein | 166 | 59% helix, 14% strand | A5A5M5 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 5 copies · chains A, H, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 943 | 0.77 | 0.80 | 83 | empty |
| 2 | 541 | 0.68 | 0.78 | 59 | empty |
| 3 | 337 | 0.58 | 0.76 | 44 | empty |
| 4 | 369 | 0.55 | 0.74 | 48 | empty |
| 5 | 319 | 0.54 | 0.75 | 38 | empty |
Interfaces
10 interfaces between chains.
- E–F · 2269 Ų buried · 32 hydrogen bonds · protein-protein
- A–B · 2253 Ų buried · 28 hydrogen bonds · protein-protein
- G–H · 1911 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 1776 Ų buried · 13 hydrogen bonds · protein-protein
- E–G · 537 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 22 disulfide, 3 glycan (disulfide, N-glycosylation).
Compared structures
- 5A3I · Crystal Structure of a Complex formed between FLD194 Fab and Transmissible Mutant H5… · 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 A5A5M5
- Elsewhere: RCSB PDB 5A3I · PDBe 5A3I · UniProt A5A5M5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.