MolNFT v1 · #182764 · protein
Crystal structure of an anti-SARS-cov-2 human neutralizing antibody Fab fragment C099
7N3H · C099 Fab heavy chain: “Crystal structure of an anti-SARS-cov-2 human neutralizing antibody Fab fragment C099”. X-ray diffraction, 5 pockets (best druggability 0.53). MolNFT v1 #182764 on GenesisL1: 3D structure, binding sites and…
- PDB
- 7N3H
- Type
- protein
- Length
- 427 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- C099 Fab heavy chain; C099 Fab light chain
- Pockets
- 5 · best druggability 0.53
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | C099 Fab heavy chain | protein | 214 | 8% helix, 52% strand | — |
| L | C099 Fab light chain | protein | 213 | 8% helix, 51% strand | — |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 328 | 0.53 | 0.74 | 45 | empty |
| 2 | 51 | 0.53 | 0.89 | 18 | empty |
| 3 | 122 | 0.36 | 0.73 | 17 | empty |
| 4 | 100 | 0.33 | 0.73 | 20 | empty |
| 5 | 63 | 0.29 | 0.73 | 19 | empty |
Interfaces
1 interface between chains.
- H–L · 1812 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 7N3H · Crystal structure of an anti-SARS-CoV-2 human neutralizing antibody Fab fragment C099 · the same entry in another collection · chain H against H, 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
- Elsewhere: RCSB PDB 7N3H · PDBe 7N3H
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.