Research workbench
HA1.7 human T-cell receptor specific for influenza virus epitope pkyvkqntlklat presented by human leukocyte antigen HLA-DR0101
Analyse HA1.7 human T-cell receptor specific for influenza virus epitope pkyvkqntlklat… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FR6
- Type
- protein
- Length
- 443 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Human T-cell receptor alpha chain; Human T-cell receptor beta chain
- Ligands
- SO4
- Pockets
- 3 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 5% helix, 45% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Human T-cell receptor alpha chain | protein | 202 | 3% helix, 45% strand | — |
| B | Human T-cell receptor beta chain | protein | 241 | 6% helix, 45% strand | — |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 993 | 0.71 | 0.75 | 76 | empty |
| 2 | 71 | 0.41 | 0.80 | 21 | empty |
| 3 | 68 | 0.33 | 0.75 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 2151 Ų buried · 25 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 5 disulfide (disulfide).
Compared structures
- 6FR6 · HA1.7 Human T-Cell Receptor specific for Influenza virus epitope PKYVKQNTLKLAT presented… · the same entry in another collection · chain A against A, 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 6FR6 · PDBe 6FR6
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