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Crystal structure of 26S proteasome subunit RPN2

Analyse Crystal structure of 26S proteasome subunit RPN2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4ADY
Type
protein
Length
1,651 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
26S proteasome regulatory subunit RPN2
UniProt
P32565
Pockets
10 · best druggability 0.85

Structure

x-ray diffraction · 2 distinct chains · 64% helix, 5% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A26S proteasome regulatory subunit RPN2protein84964% helix, 5% strandP32565
B26S proteasome regulatory subunit RPN2protein80263% helix, 5% strandP32565

Pockets

10 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110700.850.86110empty
211990.820.83129empty
34680.680.7935empty
41890.520.7825empty
51050.510.8216empty

Interfaces

1 interface between chains.

  • A–B · 907 Ų buried · 6 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 40 modified (engineered).

Compared structures

  • 4ADY · Crystal structure of 26S proteasome subunit Rpn2 · the same entry in another collection · chain A against A, TM-score 1.00
  • P32565 · AlphaFold monomer V2.0 prediction for 26S proteasome regulatory subunit RPN2 (P32565) · a predicted model of the same protein · chain B against A, TM-score 0.99

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