Research workbench
Structure of the broadly neutralizing antibody HC1AM
Analyse Structure of the broadly neutralizing antibody HC1AM in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WOR
- Type
- protein
- Length
- 426 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Fab HC1AM heavy chain; Fab HC1AM light chain
- Pockets
- 5 · best druggability 0.64
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | Fab HC1AM heavy chain | protein | 214 | 7% helix, 51% strand | — |
| L | Fab HC1AM light chain | protein | 212 | 7% helix, 50% 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 | 101 | 0.64 | 0.88 | 22 | empty |
| 2 | 474 | 0.58 | 0.74 | 54 | empty |
| 3 | 124 | 0.38 | 0.74 | 20 | empty |
| 4 | 94 | 0.36 | 0.75 | 24 | empty |
| 5 | 58 | 0.27 | 0.73 | 24 | empty |
Interfaces
1 interface between chains.
- H–L · 1824 Ų buried · 15 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6WOR · Structure of the broadly neutralizing antibody HC1AM · 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 6WOR · PDBe 6WOR
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