Research workbench
The three-dimensional structure of a class I major histocompatibility complex molecule missing the ALPHA3 domain of the heavy chain
Analyse The three-dimensional structure of a class I major histocompatibility complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1TMC
- Type
- protein
- Length
- 284 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Class I histocompatibility antigen (HLA-AW68); Beta 2-microglobulin; Decameric peptide…
- UniProt
- P01891, P61769
- Pockets
- 1 · best druggability 0.44
Structure
x-ray diffraction · 3 distinct chains · 24% helix, 37% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Class I histocompatibility antigen (HLA-AW68) | protein | 175 | 38% helix, 32% strand | P01891 |
| B | Beta 2-microglobulin | protein | 99 | 0% helix, 49% strand | P61769 |
| C | Decameric peptide (evappeyhrk) | protein | 10 | 0% helix, 0% strand | — |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 150 | 0.44 | 0.76 | 23 | empty |
Interfaces
2 interfaces between chains.
- A–C · 938 Ų buried · 17 hydrogen bonds · protein-protein
- A–B · 710 Ų buried · 12 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 2 disulfide (disulfide).
Compared structures
- 1TMC · The three-dimensional structure of a class I major histocompatibility complex molecule… · 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 P01891
- Every structure of UniProt P61769
- Elsewhere: RCSB PDB 1TMC · PDBe 1TMC · UniProt P01891 · UniProt P61769
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