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Crystal structure of archaeal 20S proteasome in complex with mutated P26 activator

Analyse Crystal structure of archaeal 20S proteasome in complex with mutated P26… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3JTL
Type
protein
Length
4,536 residues
Chains
21
Method
x-ray diffraction
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, Q9U8G2
Pockets
20 · best druggability 0.80

Structure

x-ray diffraction · 3 distinct chains · 48% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, F, GProteasome subunit alpha (EC 3.4.25.1)protein22733% helix, 26% strandP25156
H, I, J, K, L, M, NProteasome subunit beta (EC 3.4.25.1)protein20337% helix, 30% strandP28061
O, P, Q, R, S, T, UProteasome activator protein PA26protein21873% helix, 1% strandQ9U8G2

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111360.800.81136empty
211740.800.81139empty
38680.780.81107empty
48640.760.80105empty
55490.750.8381empty

Interfaces

56 interfaces between chains.

  • S–T · 2193 Ų buried · 38 hydrogen bonds · protein-protein
  • Q–R · 2172 Ų buried · 34 hydrogen bonds · protein-protein
  • P–Q · 2172 Ų buried · 34 hydrogen bonds · protein-protein
  • O–P · 2171 Ų buried · 34 hydrogen bonds · protein-protein
  • R–S · 2160 Ų buried · 32 hydrogen bonds · protein-protein

Compared structures

  • 3JTL · Crystal structure of archaeal 20S proteasome in complex with mutated P26 activator · the same entry in another collection · chain U against U, TM-score 1.00

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