Research workbench
Allosteric coupling between alpha-rings of the 20S proteasome, 20S singly capped with a PA26/V230F
Analyse Allosteric coupling between alpha-rings of the 20S proteasome, 20S singly… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UTG
- Type
- protein
- Length
- 7,525 residues
- Chains
- 35
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Proteasome subunit beta; Proteasome subunit alpha; Proteasome activator protein PA26
- EC
- 3.4.25.1
- UniProt
- P28061, P25156, Q9U8G2
- Pockets
- 20 · best druggability 0.83
Structure
electron microscopy · 4 distinct chains · 45% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1, 2, H, I, J, K, L, M, N, V, W, X, Y, Z | Proteasome subunit beta (EC 3.4.25.1) | protein | 203 | 37% helix, 26% strand | P28061 |
| A, B, C, D, E, F, G | Proteasome subunit alpha (EC 3.4.25.1) | protein | 227 | 33% helix, 24% strand | P25156 |
| O, P, Q, R, S, T, U | Proteasome activator protein PA26 | protein | 218 | 72% helix, 1% strand | Q9U8G2 |
| a, b, c, d, e, f, g | Proteasome subunit alpha (EC 3.4.25.1) | protein | 224 | 37% helix, 26% strand | P25156 |
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 | 1102 | 0.83 | 0.84 | 98 | empty |
| 2 | 1167 | 0.82 | 0.83 | 110 | empty |
| 3 | 1140 | 0.82 | 0.83 | 119 | empty |
| 4 | 1089 | 0.82 | 0.83 | 107 | empty |
| 5 | 1173 | 0.82 | 0.83 | 115 | empty |
Interfaces
98 interfaces between chains.
- O–P · 2212 Ų buried · 33 hydrogen bonds · protein-protein
- R–S · 2207 Ų buried · 35 hydrogen bonds · protein-protein
- T–U · 2204 Ų buried · 33 hydrogen bonds · protein-protein
- O–U · 2204 Ų buried · 33 hydrogen bonds · protein-protein
- S–T · 2203 Ų buried · 32 hydrogen bonds · protein-protein
Compared structures
- 6UTG · Allosteric coupling between alpha-rings of the 20S proteasome, 20S singly capped with a… · the same entry in another collection · chain I against I, 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 P28061
- Every structure of UniProt P25156
- Every structure of UniProt Q9U8G2
- Elsewhere: RCSB PDB 6UTG · PDBe 6UTG · UniProt P28061 · UniProt P25156 · UniProt Q9U8G2
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