Research workbench
Complex (ANTIBODY/ANTIGEN)
Analyse Complex (ANTIBODY/ANTIGEN) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1JRH
- Type
- protein
- Length
- 442 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Antibody A6; Interferon-gamma receptor alpha chain
- UniProt
- P15260
- Pockets
- 3 · best druggability 0.58
Structure
x-ray diffraction · 3 distinct chains · 3% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| L | Antibody A6 | protein | 167 | 2% helix, 45% strand | — |
| H | Antibody A6 | protein | 180 | 5% helix, 46% strand | — |
| I | Interferon-gamma receptor alpha chain | protein | 95 | 3% helix, 48% strand | P15260 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 408 | 0.58 | 0.75 | 56 | empty |
| 2 | 113 | 0.43 | 0.77 | 23 | empty |
| 3 | 106 | 0.42 | 0.77 | 19 | empty |
Interfaces
3 interfaces between chains.
- L–H · 1174 Ų buried · 10 hydrogen bonds · protein-protein
- H–I · 486 Ų buried · 16 hydrogen bonds · protein-protein
- L–I · 475 Ų buried · 6 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt P15260
- Elsewhere: RCSB PDB 1JRH · PDBe 1JRH · UniProt P15260
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.