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Yeast 26S proteasome bound to ubiquitinated substrate (5T motor state)

Analyse Yeast 26S proteasome bound to ubiquitinated substrate (5T motor state) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6EF2
Type
protein
Length
3,290 residues
Chains
14
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Proteasome subunit alpha type-1; Proteasome subunit alpha type-2; Proteasome subunit…
EC
3.4.25.1
UniProt
P21243, P23639, P23638, P40303, P32379, P40302, P21242, P33299, P40327, Q01939, P33298, P53549, P33297
Ligands
ATP, ADP
Pockets
20 · best druggability 0.83

Structure

electron microscopy · 14 distinct chains · 35% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProteasome subunit alpha type-1 (EC 3.4.25.1)protein23832% helix, 18% strandP21243
BProteasome subunit alpha type-2 (EC 3.4.25.1)protein24928% helix, 18% strandP23639
CProteasome subunit alpha type-3 (EC 3.4.25.1)protein24131% helix, 15% strandP23638
DProteasome subunit alpha type-4 (EC 3.4.25.1)protein24132% helix, 17% strandP40303
EProteasome subunit alpha type-5 (EC 3.4.25.1)protein24732% helix, 15% strandP32379
FProteasome subunit alpha type-6 (EC 3.4.25.1)protein23229% helix, 22% strandP40302
GProbable proteasome subunit alpha type-7 (EC 3.4.25.1)protein24634% helix, 20% strandP21242
H26S proteasome regulatory subunit 7 homologprotein26540% helix, 9% strandP33299
I26S proteasome regulatory subunit 4 homologprotein26037% helix, 6% strandP40327
J26S proteasome regulatory subunit 8 homologprotein26238% helix, 10% strandQ01939
K26S proteasome regulatory subunit 6B homologprotein25938% helix, 5% strandP33298
L26S proteasome subunit RPT4protein26444% helix, 5% strandP53549
M26S proteasome regulatory subunit 6Aprotein27040% helix, 9% strandP33297
sModel substrate polypeptideprotein160% helix, 0% strand—

Ligands and binding sites

  • ATP · Adenosine-5'-triphosphate · ligand · 4 copies · chains H, I, J, K, M
  • ADP · Adenosine-5'-diphosphate · ligand · 2 copies · chains K, L

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111060.830.84117ATP
24780.810.8872empty
33620.800.8953empty
47140.800.8484ATP
511270.780.8097empty

Interfaces

35 interfaces between chains.

  • J–K · 1835 Ų buried · 12 hydrogen bonds · protein-protein
  • H–I · 1768 Ų buried · 17 hydrogen bonds · protein-protein
  • I–J · 1709 Ų buried · 10 hydrogen bonds · protein-protein
  • C–D · 1389 Ų buried · 17 hydrogen bonds · protein-protein
  • D–E · 1344 Ų buried · 22 hydrogen bonds · protein-protein

Compared structures

  • 6EF2 · Yeast 26S proteasome bound to ubiquitinated substrate (5T motor state) · the same entry in another collection · chain s against s, TM-score 1.00

Analyse

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