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2.8 a resolution reconstruction of the thermoplasma acidophilum 20S proteasome using cryo-electron microscopy

Analyse 2.8 a resolution reconstruction of the 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
6BDF
Type
protein
Length
5,908 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 · 36% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, E, G, I, K, M, O, Q, S, U, W, Y, 0Proteasome subunit alpha (EC 3.4.25.1)protein22136% helix, 27% strandP25156
B, D, F, H, J, L, N, P, R, T, V, X, Z, 1Proteasome subunit beta (EC 3.4.25.1)protein20135% helix, 30% strandP28061

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19860.760.78103empty
27540.760.8071empty
37210.750.8169empty
47520.750.8071empty
57310.750.8070empty

Interfaces

70 interfaces between chains.

  • O–Q · 1274 Ų buried · 24 hydrogen bonds · protein-protein
  • Q–S · 1274 Ų buried · 24 hydrogen bonds · protein-protein
  • Y–0 · 1273 Ų buried · 24 hydrogen bonds · protein-protein
  • S–U · 1270 Ų buried · 24 hydrogen bonds · protein-protein
  • E–G · 1270 Ų buried · 24 hydrogen bonds · protein-protein

Compared structures

  • 6BDF · 2.8 A resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using… · the same entry in another collection · chain K against K, TM-score 1.00

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