Research workbench
Structure of a nested set of N-terminally extended MHC I-peptides provides novel insights into antigen processing and presentation
Analyse Structure of a nested set of N-terminally extended MHC I-peptides provides… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6P27
- Type
- protein
- Length
- 384 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- HLA class I histocompatibility antigen, B-8 alpha chain; Beta-2-microglobulin; MHC…
- UniProt
- P30460, P61769
- Pockets
- 6 · best druggability 0.68
Structure
x-ray diffraction · 3 distinct chains · 19% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | HLA class I histocompatibility antigen, B-8 alpha chain | protein | 276 | 26% helix, 39% strand | P30460 |
| B | Beta-2-microglobulin | protein | 99 | 0% helix, 49% strand | P61769 |
| C | MHC I-peptide | protein | 9 | 0% helix, 0% strand | — |
Pockets
6 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 589 | 0.68 | 0.77 | 51 | empty |
| 2 | 100 | 0.44 | 0.79 | 23 | empty |
| 3 | 98 | 0.40 | 0.77 | 22 | empty |
| 4 | 75 | 0.39 | 0.78 | 16 | empty |
| 5 | 53 | 0.30 | 0.76 | 14 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1337 Ų buried · 23 hydrogen bonds · protein-protein
- A–C · 888 Ų buried · 18 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 6P27 · Structure of a nested set of N-terminally extended MHC I-peptides provides novel insights… · the same entry in another collection · chain A against A, TM-score 1.00
- P61769 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P61769) · a predicted model of the same protein · chain B against A, TM-score 0.98
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 P30460
- Every structure of UniProt P61769
- Elsewhere: RCSB PDB 6P27 · PDBe 6P27 · UniProt P30460 · UniProt P61769
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