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UniProt Q12250

26S proteasome regulatory subunit RPN5 (Q12250)

26S proteasome regulatory subunit RPN5 (UniProt Q12250): 31 experimental structures and 1 predicted model on GenesisL1, 6 pockets. Binding sites, druggability and experiment against prediction (TM-score) in GL1X.

UniProt
Q12250
Protein
26S proteasome regulatory subunit RPN5
Experimental structures
31
Predicted models
1
Pockets
6 · 2 records with a druggable one

Structures

32 records of Q12250 in the MolNFT archive: 31 experimental, 1 predicted.

EntryTitleMethodChainsLigandsPockets
3J47Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lidelectron microscopyP——
3J47Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lidelectron microscopyP——
3JCKStructure of the yeast 26S proteasome lid sub-complexelectron microscopyB——
3JCKStructure of the yeast 26S proteasome lid sub-complexelectron microscopyB——
3JCOStructure of yeast 26S proteasome in M1 state derived from Titan datasetelectron microscopyP——
3JCPStructure of yeast 26S proteasome in M2 state derived from Titan datasetelectron microscopyP——
4CR2Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S…electron microscopyP——
4CR2Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S…electron microscopyP——
4CR3Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S…electron microscopyP——
4CR3Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S…electron microscopyP——
4CR4Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S…electron microscopyP——
4CR4Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S…electron microscopyP——
5A5BStructure of the 26S proteasome-Ubp6 complexelectron microscopyP——
5A5BStructure of the 26S proteasome-UBP6 complexelectron microscopyP——
5MPB26S proteasome in presence of AMP-PNP (s3)electron microscopyP——
5MPC26S proteasome in presence of BeFx (s4)electron microscopyP——
5MPD26S proteasome in presence of ATP (s1)electron microscopyP—2 (best 0.77)
5MPD26S proteasome in presence of ATP (S1)electron microscopyP——
5MPE26S proteasome in presence of ATP (s2)electron microscopyP——
5MPE26S proteasome in presence of ATP (S2)electron microscopyP——
5WVIThe resting state of yeast proteasomeelectron microscopyP——
5ZMRSolution Structure of the N-terminal Domain of the Yeast Rpn5solution nmrA—1 (best 0.32)
5ZMRSolution structure of the N-terminal domain of the yeast RPN5solution nmrA——
6FVT26S proteasome, s1 stateelectron microscopyP——
6FVU26S proteasome, s2 stateelectron microscopyP——
6FVV26S proteasome, s3 stateelectron microscopyP——
6FVW26S proteasome, s4 stateelectron microscopyP——
6J2CYeast proteasome in translocation competent state (C3-a)electron microscopyP——
6J2XYeast proteasome in resting state (C1-a)electron microscopyP——
7QO3Structure of the 26S proteasome-Ubp6 complex in the si state (Core Particle and Lid)electron microscopyP—1 (best 0.71)
7QO3Structure of the 26S proteasome-UBP6 complex in the si state (core particle and lid)electron microscopyP——
Q12250AlphaFold monomer V2.0 prediction for 26S proteasome regulatory subunit RPN5 (Q12250)predictedA—2 (best 0.30)

Experiment against prediction

Elsewhere

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