MolNFT v1 · #149840 · protein
Ablift: antibody stability and affinity optimization by computational design of the variable light-heavy chain interface
6GC2 · Light chain: “Ablift: antibody stability and affinity optimization by computational design of the variable light-heavy…”. X-ray diffraction, 3 pockets (best druggability 0.61). MolNFT v1 #149840 on GenesisL1: 3D structure, binding…
- PDB
- 6GC2
- Type
- protein
- Length
- 427 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Light chain; Heavy chain
- Pockets
- 3 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 7% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Light chain | protein | 214 | 6% helix, 50% strand | — |
| H | Heavy chain | protein | 213 | 9% helix, 50% strand | — |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 413 | 0.61 | 0.76 | 54 | empty |
| 2 | 246 | 0.54 | 0.77 | 30 | empty |
| 3 | 54 | 0.25 | 0.73 | 12 | empty |
Interfaces
1 interface between chains.
- L–H · 1781 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6GC2 · AbLIFT: Antibody stability and affinity optimization by computational design of the… · 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
- Elsewhere: RCSB PDB 6GC2 · PDBe 6GC2
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