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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
- 1YPZ
- Type
- protein
- Length
- 1,598 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- H2-T22 protein; Beta-2-microglobulin; T cell receptor delta; T-cell receptor gamma chain
- UniProt
- P61769
- Ligands
- NAG, MAN, FUC
- Pockets
- 20 · best druggability 0.70
Structure
x-ray diffraction · 4 distinct chains · 8% helix, 43% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | H2-T22 protein | protein | 260 | 15% helix, 35% strand | — |
| B, D | Beta-2-microglobulin | protein | 102 | 0% helix, 46% strand | P61769 |
| E, G | T cell receptor delta | protein | 207 | 1% helix, 52% strand | — |
| F, H | T-cell receptor gamma chain | protein | 230 | 8% helix, 43% strand | — |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 10 copies · chains E, F, G, H
- MAN · alpha-D-mannopyranose · sugar · 2 copies · chains F, H
- FUC · alpha-L-fucopyranose · sugar · chains G
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 969 | 0.70 | 0.75 | 91 | empty |
| 2 | 599 | 0.69 | 0.78 | 51 | empty |
| 3 | 479 | 0.68 | 0.79 | 62 | empty |
| 4 | 595 | 0.67 | 0.77 | 48 | empty |
| 5 | 426 | 0.65 | 0.78 | 51 | empty |
Interfaces
12 interfaces between chains.
- E–F · 1838 Ų buried · 10 hydrogen bonds · protein-protein
- G–H · 1751 Ų buried · 11 hydrogen bonds · protein-protein
- A–B · 1373 Ų buried · 15 hydrogen bonds · protein-protein
- C–D · 1354 Ų buried · 21 hydrogen bonds · protein-protein
- C–G · 930 Ų buried · 10 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 14 disulfide, 6 glycan (disulfide, N-glycosylation, glycosylation).
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 P61769
- Elsewhere: RCSB PDB 1YPZ · PDBe 1YPZ · UniProt P61769
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