Research workbench
24B3 antibody-peptide complex
Analyse 24B3 antibody-peptide complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7Y3J
- Type
- protein
- Length
- 447 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 24B3 light chain; 24B3 heavy chain; Ala-leu-val-phe-phe-ala-pro-ala-val-gly-ser
- Pockets
- 5 · best druggability 0.59
Structure
x-ray diffraction · 3 distinct chains · 6% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | 24B3 light chain | protein | 217 | 6% helix, 52% strand | — |
| H | 24B3 heavy chain | protein | 219 | 7% helix, 50% strand | — |
| A | Ala-leu-val-phe-phe-ala-pro-ala-val-gly-ser | protein | 11 | 0% helix, 9% strand | — |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 488 | 0.59 | 0.74 | 58 | empty |
| 2 | 151 | 0.46 | 0.76 | 20 | empty |
| 3 | 127 | 0.42 | 0.75 | 21 | empty |
| 4 | 84 | 0.37 | 0.76 | 17 | empty |
| 5 | 53 | 0.25 | 0.73 | 19 | empty |
Interfaces
3 interfaces between chains.
- L–H · 1872 Ų buried · 18 hydrogen bonds · protein-protein
- H–A · 412 Ų buried · 4 hydrogen bonds · protein-protein
- L–A · 371 Ų buried · 3 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 7Y3J · 24B3 antibody-peptide complex · 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 7Y3J · PDBe 7Y3J
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