Research workbench
HLA-TCR complex
Analyse HLA-TCR complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6PY2
- Type
- protein
- Length
- 806 residues
- Chains
- 5
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q08AS3, A0A0U5IHY9, K7N5N2, K7N5M4
- Ligands
- NAG
Structure
x-ray diffraction · 5 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 182 | — | Q08AS3 |
| B | — | protein | 178 | — | A0A0U5IHY9 |
| C | — | protein | 12 | — | — |
| D | — | protein | 191 | — | K7N5N2 |
| E | — | protein | 243 | — | K7N5M4 |
Ligands and binding sites
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A, B
- GOL · Glycerol · additive · 2 copies · chains A, B, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6PY2 · HLA-TCR complex · 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
- Every structure of UniProt Q08AS3
- Every structure of UniProt A0A0U5IHY9
- Every structure of UniProt K7N5N2
- Every structure of UniProt K7N5M4
- Elsewhere: RCSB PDB 6PY2 · PDBe 6PY2 · UniProt Q08AS3 · UniProt A0A0U5IHY9 · UniProt K7N5N2 · UniProt K7N5M4
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