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Proteasome from thermoplasma acidophilum

Analyse Proteasome from thermoplasma acidophilum in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1PMA
Type
protein
Length
5,936 residues
Chains
28
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Proteasome
EC
3.4.99.46
UniProt
P25156, P28061
Pockets
20 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 38% helix, 30% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, C, D, E, F, G, H, I, J, K, L, M, N, OProteasome (EC 3.4.99.46)protein22139% helix, 28% strandP25156
B, P, Q, R, S, T, U, V, W, X, Y, Z, 1, 2Proteasome (EC 3.4.99.46)protein20337% helix, 32% strandP28061

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17940.760.8078empty
27650.750.8073empty
37990.750.8082empty
47860.750.8080empty
57010.740.8071empty

Interfaces

70 interfaces between chains.

  • I–J · 1300 Ų buried · 26 hydrogen bonds · protein-protein
  • L–M · 1297 Ų buried · 25 hydrogen bonds · protein-protein
  • E–F · 1292 Ų buried · 25 hydrogen bonds · protein-protein
  • A–H · 1292 Ų buried · 25 hydrogen bonds · protein-protein
  • I–O · 1276 Ų buried · 23 hydrogen bonds · protein-protein

Compared structures

  • 1PMA · Proteasome from thermoplasma acidophilum · the same entry in another collection · chain H against H, TM-score 1.00

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