Research workbench
Immune receptor
Analyse Immune receptor in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4GG8
- Type
- protein
- Length
- 836 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- T-cell receptor, SP3.4 alpha chain; T-cell receptor, SP3.4 beta chain
- Ligands
- GLC, FRU
- Pockets
- 8 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 46% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| E, A | T-cell receptor, SP3.4 alpha chain | protein | 174 | 2% helix, 43% strand | — |
| F, B | T-cell receptor, SP3.4 beta chain | protein | 244 | 7% helix, 49% strand | — |
Ligands and binding sites
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains E, A
- FRU · beta-D-fructofuranose · sugar · 2 copies · chains A, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1022 | 0.71 | 0.75 | 108 | empty |
| 2 | 1025 | 0.70 | 0.74 | 92 | empty |
| 3 | 185 | 0.50 | 0.77 | 29 | GLC |
| 4 | 151 | 0.50 | 0.78 | 28 | empty |
| 5 | 76 | 0.35 | 0.76 | 17 | empty |
Interfaces
3 interfaces between chains.
- E–F · 1819 Ų buried · 15 hydrogen bonds · protein-protein
- B–A · 1742 Ų buried · 14 hydrogen bonds · protein-protein
- E–A · 713 Ų buried · 16 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 disulfide (disulfide).
Compared structures
- 4GG8 · Immune Receptor · the same entry in another collection · chain E against E, 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 4GG8 · PDBe 4GG8
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