Research workbench
Antibody multispecificity mediated by conformational diversity
Analyse Antibody multispecificity mediated by conformational diversity in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1OAY
- Type
- protein
- Length
- 634 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Immunoglobulin E
- Ligands
- FUR
- Pockets
- 7 · best druggability 0.64
Structure
x-ray diffraction · 5 distinct chains · 1% helix, 42% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| H, J | Immunoglobulin E | protein | 121 | 5% helix, 49% strand | — |
| L | Immunoglobulin E | protein | 108 | 0% helix, 44% strand | — |
| M | Immunoglobulin E | protein | 85 | 0% helix, 33% strand | — |
| N | Immunoglobulin E | protein | 107 | 0% helix, 50% strand | — |
| O | Immunoglobulin E | protein | 92 | 0% helix, 33% strand | — |
Ligands and binding sites
- FUR · Furazolidone · ligand · 2 copies · chains H, L, O, J, M, N
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 77 | 0.64 | 0.91 | 23 | empty |
| 2 | 197 | 0.57 | 0.80 | 32 | FUR |
| 3 | 242 | 0.57 | 0.78 | 24 | empty |
| 4 | 154 | 0.53 | 0.79 | 29 | FUR |
| 5 | 154 | 0.43 | 0.75 | 26 | empty |
Interfaces
6 interfaces between chains.
- J–N · 934 Ų buried · 10 hydrogen bonds · protein-protein
- H–L · 931 Ų buried · 9 hydrogen bonds · protein-protein
- H–O · 235 Ų buried · 2 hydrogen bonds · protein-protein
- J–M · 202 Ų buried · 2 hydrogen bonds · protein-protein
- M–N · 41 Ų buried · 0 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 6 disulfide (disulfide).
Compared structures
- 1OAY · Antibody multispecificity mediated by conformational diversity · 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 1OAY · PDBe 1OAY
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