MolNFT v1 · #147069 · protein
HLA-A*0201 single chain trimer with murine H2K alpha 3 domain and HPV.16 E7 peptide ymldlqpet
6E1I: “HLA-A*0201 single chain trimer with murine H2K alpha 3 domain and HPV.16 E7 peptide ymldlqpet”. X-ray diffraction, 3 pockets (best druggability 0.68). MolNFT v1 #147069 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6E1I
- Type
- protein
- Length
- 389 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HLA-A*0201 single chain trimer with murine H2K alpha 3 domain and HPV.16 E7 peptide…
- UniProt
- P01887, P01892, P01902
- Pockets
- 3 · best druggability 0.68
Structure
x-ray diffraction · 1 distinct chain · 20% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HLA-A*0201 single chain trimer with murine H2K alpha 3 domain and HPV.16 E7 peptide ymldlqpet | protein | 389 | 20% helix, 41% strand | P01887, P01892, P01902 |
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 652 | 0.68 | 0.76 | 62 | empty |
| 2 | 236 | 0.51 | 0.75 | 36 | empty |
| 3 | 103 | 0.41 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 6E1I · HLA-A*0201 single chain trimer with murine H2K alpha 3 domain and HPV.16 E7 peptide… · the same entry in another collection · chain A against A, TM-score 1.00
- P01902 · AlphaFold monomer V2.0 prediction for H-2 class I histocompatibility antigen, K-D alpha… · a predicted model of the same protein · chain A against A, TM-score 0.69
- P01887 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P01887) · a predicted model of the same protein · chain A against A, TM-score 0.25
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 P01887
- Every structure of UniProt P01892
- Every structure of UniProt P01902
- Elsewhere: RCSB PDB 6E1I · PDBe 6E1I · UniProt P01887 · UniProt P01892 · UniProt P01902
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