Research workbench
Crystal structure of vaccine-elicited pan- influenza H1N1 neutralizing murine antibody 441D6.
Analyse Crystal structure of vaccine-elicited pan- influenza H1N1 neutralizing murine… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5TR8
- Type
- protein
- Length
- 432 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 441D6 Fab light chain; 441D6 Fab heavy chain
- UniProt
- Q7TS98, A0A0E4B366
- Ligands
- NI
- Pockets
- 6 · best druggability 0.57
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 52% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | 441D6 Fab light chain | protein | 212 | 6% helix, 51% strand | Q7TS98 |
| H | 441D6 Fab heavy chain | protein | 220 | 5% helix, 52% strand | A0A0E4B366 |
Ligands and binding sites
- NI · Nickel (II) ion · metal · 2 copies · chains L, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 372 | 0.57 | 0.75 | 48 | empty |
| 2 | 109 | 0.39 | 0.75 | 21 | empty |
| 3 | 133 | 0.38 | 0.73 | 23 | empty |
| 4 | 85 | 0.37 | 0.76 | 22 | empty |
| 5 | 120 | 0.37 | 0.73 | 24 | empty |
Interfaces
1 interface between chains.
- L–H · 1797 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 5TR8 · Crystal structure of vaccine-elicited pan- influenza H1N1 neutralizing murine antibody… · the same entry in another collection · chain L against L, 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 Q7TS98
- Every structure of UniProt A0A0E4B366
- Elsewhere: RCSB PDB 5TR8 · PDBe 5TR8 · UniProt Q7TS98 · UniProt A0A0E4B366
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