Research workbench
SARS-cov-2 rlq peptide-specific TCR PRLQ3 binds to rlq-HLA-A2
Analyse SARS-cov-2 rlq peptide-specific TCR PRLQ3 binds to rlq-HLA-A2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N1E
- Type
- protein
- Length
- 826 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- MHC class I antigen, a-2 alpha chain; Beta-2-microglobulin; Spike protein S2; PRLQ3 T…
- UniProt
- A0A5B8RNS7, P61769, P0DTC2
- Pockets
- 10 · best druggability 0.76
Structure
x-ray diffraction · 5 distinct chains · 13% helix, 44% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | MHC class I antigen, a-2 alpha chain | protein | 274 | 28% helix, 39% strand | A0A5B8RNS7 |
| B | Beta-2-microglobulin | protein | 100 | 0% helix, 49% strand | P61769 |
| C | Spike protein S2 | protein | 9 | 0% helix, 0% strand | P0DTC2 |
| D | PRLQ3 T cell receptor alpha chain | protein | 200 | 6% helix, 43% strand | — |
| E | PRLQ3 T cell receptor beta chain | protein | 243 | 7% helix, 49% strand | — |
Pockets
10 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1058 | 0.76 | 0.78 | 82 | empty |
| 2 | 558 | 0.68 | 0.78 | 52 | empty |
| 3 | 149 | 0.51 | 0.79 | 22 | empty |
| 4 | 193 | 0.48 | 0.76 | 40 | empty |
| 5 | 69 | 0.47 | 0.83 | 18 | empty |
Interfaces
7 interfaces between chains.
- D–E · 2224 Ų buried · 26 hydrogen bonds · protein-protein
- A–B · 1380 Ų buried · 27 hydrogen bonds · protein-protein
- A–C · 889 Ų buried · 17 hydrogen bonds · protein-protein
- A–E · 343 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 286 Ų buried · 4 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 8 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 A0A5B8RNS7
- Every structure of UniProt P61769
- Every structure of UniProt P0DTC2
- Elsewhere: RCSB PDB 7N1E · PDBe 7N1E · UniProt A0A5B8RNS7 · UniProt P61769 · UniProt P0DTC2
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