Research workbench
Thermoplasma acidophilum 20S proteasome
Analyse Thermoplasma acidophilum 20S proteasome in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3J9I
- Type
- protein
- Length
- 5,978 residues
- Chains
- 28
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteasome subunit alpha; Proteasome subunit beta
- EC
- 3.4.25.1
- UniProt
- P25156, P28061
- Pockets
- 20 · best druggability 0.75
Structure
electron microscopy · 2 distinct chains · 38% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| S, F, T, G, U, A, O, B, P, C, Q, D, R, E | Proteasome subunit alpha (EC 3.4.25.1) | protein | 224 | 39% helix, 25% strand | P25156 |
| Z, M, 1, N, 2, H, V, I, W, J, X, K, Y, L | Proteasome subunit beta (EC 3.4.25.1) | protein | 203 | 37% helix, 28% strand | P28061 |
Pockets
20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 723 | 0.75 | 0.80 | 83 | empty |
| 2 | 711 | 0.75 | 0.80 | 75 | empty |
| 3 | 705 | 0.75 | 0.80 | 77 | empty |
| 4 | 731 | 0.75 | 0.80 | 80 | empty |
| 5 | 698 | 0.75 | 0.80 | 84 | empty |
Interfaces
70 interfaces between chains.
- F–G · 1451 Ų buried · 26 hydrogen bonds · protein-protein
- O–P · 1449 Ų buried · 26 hydrogen bonds · protein-protein
- Q–R · 1449 Ų buried · 26 hydrogen bonds · protein-protein
- U–O · 1448 Ų buried · 26 hydrogen bonds · protein-protein
- D–E · 1448 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 3J9I · Thermoplasma acidophilum 20S proteasome · 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 P25156
- Every structure of UniProt P28061
- Elsewhere: RCSB PDB 3J9I · PDBe 3J9I · UniProt P25156 · UniProt P28061
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.