Research workbench
Crystal structure of broadly neutralizing antibody HEPC3.1
Analyse Crystal structure of broadly neutralizing antibody HEPC3.1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7U0B
- Type
- protein
- Length
- 433 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HEPC3.1 Fab heavy chain; HEPC3.1 Fab light chain
- Pockets
- 5 · best druggability 0.63
Structure
x-ray diffraction · 2 distinct chains · 6% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H | HEPC3.1 Fab heavy chain | protein | 221 | 7% helix, 51% strand | — |
| L | HEPC3.1 Fab light chain | protein | 212 | 6% helix, 52% 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 | 152 | 0.63 | 0.86 | 29 | empty |
| 2 | 433 | 0.56 | 0.73 | 53 | empty |
| 3 | 92 | 0.35 | 0.74 | 23 | empty |
| 4 | 76 | 0.34 | 0.75 | 17 | empty |
| 5 | 66 | 0.31 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- H–L · 1800 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 7U0B · Crystal structure of broadly neutralizing antibody HEPC3.1 · 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 7U0B · PDBe 7U0B
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