Research workbench
Thermoplasma acidophilum 20S proteasome with a closed gate
Analyse Thermoplasma acidophilum 20S proteasome with a closed gate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3C92
- 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 0.76
Structure
electron microscopy · 2 distinct chains · 38% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, O, P, Q, R, S, T, U | Proteasome subunit alpha (EC 3.4.25.1) | protein | 224 | 39% helix, 28% strand | P25156 |
| H, I, J, K, L, M, N, V, W, X, Y, Z, 1, 2 | Proteasome subunit beta (EC 3.4.25.1) | protein | 203 | 37% helix, 32% 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 | 949 | 0.76 | 0.79 | 95 | empty |
| 2 | 834 | 0.76 | 0.80 | 85 | empty |
| 3 | 791 | 0.75 | 0.80 | 79 | empty |
| 4 | 781 | 0.75 | 0.80 | 78 | empty |
| 5 | 741 | 0.75 | 0.80 | 75 | empty |
Interfaces
70 interfaces between chains.
- D–E · 1384 Ų buried · 28 hydrogen bonds · protein-protein
- R–S · 1381 Ų buried · 28 hydrogen bonds · protein-protein
- O–U · 1377 Ų buried · 28 hydrogen bonds · protein-protein
- A–G · 1377 Ų buried · 28 hydrogen bonds · protein-protein
- E–F · 1371 Ų buried · 26 hydrogen bonds · protein-protein
Compared structures
- 3C92 · Thermoplasma acidophilum 20S proteasome with a closed gate · the same entry in another collection · chain K against K, 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 3C92 · PDBe 3C92 · UniProt P25156 · UniProt P28061
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