Research workbench
The three-dimensional structure of H-2DB at 2.4 ångströms resolution: implications for antigen-determinant selection
Analyse The three-dimensional structure of H-2DB at 2.4 ångströms resolution… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1HOC
- Type
- protein
- Length
- 380 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Class I histocompatibility antigen (H2-db) (alpha chain); Beta 2-microglobulin; 9-residue…
- UniProt
- P01899, P01887, P26091
- Pockets
- 4 · best druggability 0.67
Structure
x-ray diffraction · 3 distinct chains · 16% helix, 35% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Class I histocompatibility antigen (H2-db) (alpha chain) | protein | 272 | 23% helix, 32% strand | P01899 |
| B | Beta 2-microglobulin | protein | 99 | 0% helix, 45% strand | P01887 |
| C | 9-residue peptide | protein | 9 | 0% helix, 0% strand | P26091 |
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 540 | 0.67 | 0.77 | 48 | empty |
| 2 | 106 | 0.43 | 0.78 | 19 | empty |
| 3 | 117 | 0.41 | 0.76 | 26 | empty |
| 4 | 65 | 0.32 | 0.76 | 13 | empty |
Interfaces
2 interfaces between chains.
- A–B · 1390 Ų buried · 21 hydrogen bonds · protein-protein
- A–C · 914 Ų buried · 26 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 3 disulfide (disulfide).
Compared structures
- 1HOC · The three-dimensional structure of H-2DB at 2.4 ångströms resolution: implications for… · the same entry in another collection · chain A against A, TM-score 1.00
- P01887 · AlphaFold monomer V2.0 prediction for beta-2-microglobulin (P01887) · 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 P01899
- Every structure of UniProt P01887
- Every structure of UniProt P26091
- Elsewhere: RCSB PDB 1HOC · PDBe 1HOC · UniProt P01899 · UniProt P01887 · UniProt P26091
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.