Research workbench
Allosteric coupling between alpha-rings of 20S proteasome, 20S proteasome singly capped with a PA26/E102A_PANC, together with lfp incubation
Analyse Allosteric coupling between alpha-rings of 20S proteasome, 20S proteasome… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UTH
- Type
- protein
- Length
- 7,553 residues
- Chains
- 35
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteasome subunit alpha; Proteasome subunit beta; Proteasome activator protein PA26
- EC
- 3.4.25.1
- UniProt
- P25156, P28061, Q38BM8
- Pockets
- 20 · best druggability 0.81
Structure
electron microscopy · 4 distinct chains · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G | Proteasome subunit alpha (EC 3.4.25.1) | protein | 227 | 37% 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, 26% strand | P28061 |
| O, P, Q, R, S, T, U | Proteasome subunit alpha (EC 3.4.25.1) | protein | 227 | 35% helix, 25% strand | P25156 |
| a, b, c, d, e, f, g | Proteasome activator protein PA26 | protein | 219 | 72% helix, 0% strand | Q38BM8 |
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 | 928 | 0.81 | 0.83 | 118 | empty |
| 2 | 225 | 0.78 | 0.92 | 26 | empty |
| 3 | 371 | 0.78 | 0.88 | 37 | empty |
| 4 | 345 | 0.77 | 0.88 | 35 | empty |
| 5 | 323 | 0.77 | 0.88 | 35 | empty |
Interfaces
98 interfaces between chains.
- a–g · 2157 Ų buried · 28 hydrogen bonds · protein-protein
- b–c · 2134 Ų buried · 21 hydrogen bonds · protein-protein
- c–d · 2127 Ų buried · 25 hydrogen bonds · protein-protein
- d–e · 2109 Ų buried · 21 hydrogen bonds · protein-protein
- f–g · 2062 Ų buried · 20 hydrogen bonds · protein-protein
Compared structures
- 6UTH · Allosteric coupling between alpha-rings of 20S proteasome, 20S proteasome singly capped… · the same entry in another collection · chain 1 against 1, 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
- Every structure of UniProt Q38BM8
- Elsewhere: RCSB PDB 6UTH · PDBe 6UTH · UniProt P25156 · UniProt P28061 · UniProt Q38BM8
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