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Allosteric coupling between alpha-rings of the 20S proteasome, archaea 20S proteasome singly capped with a pan complex

Analyse Allosteric coupling between alpha-rings of the 20S proteasome, archaea 20S… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6UTF
Type
protein
Length
6,013 residues
Chains
28
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Proteasome subunit beta; Proteasome subunit alpha
EC
3.4.25.1
UniProt
P28061, P25156
Pockets
20 · best druggability 0.78

Structure

electron microscopy · 3 distinct chains · 36% helix, 24% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
Z, M, 1, N, 2, H, V, I, W, J, X, K, Y, LProteasome subunit beta (EC 3.4.25.1)protein20337% helix, 26% strandP28061
A, B, C, D, E, F, GProteasome subunit alpha (EC 3.4.25.1)protein22735% helix, 24% strandP25156
O, P, Q, R, S, T, UProteasome subunit alpha (EC 3.4.25.1)protein22635% helix, 24% strandP25156

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17560.780.8283empty
27290.780.8272empty
37950.770.8187empty
411380.770.79112empty
511730.770.79129empty

Interfaces

70 interfaces between chains.

  • F–G · 1437 Ų buried · 19 hydrogen bonds · protein-protein
  • B–C · 1426 Ų buried · 19 hydrogen bonds · protein-protein
  • A–G · 1424 Ų buried · 20 hydrogen bonds · protein-protein
  • A–B · 1421 Ų buried · 18 hydrogen bonds · protein-protein
  • D–E · 1420 Ų buried · 17 hydrogen bonds · protein-protein

Compared structures

  • 6UTF · Allosteric coupling between alpha-rings of the 20S proteasome, archaea 20S proteasome… · the same entry in another collection · chain J against J, TM-score 1.00

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