5IRS: Proteasomal Rpn13 PRU-domain

crystal structure of the proteasomal Rpn13 PRU-domain. Determined by X-ray diffraction at 1.8 Å resolution. Released 20 Jul 2016.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Homo sapiens
Chains
1
Atoms
1,015
Mol. weight
16.92 kDa
Ligands
DTT
Released
20 Jul 2016

Explore 5IRS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5IRS contains 1 α-helix and 10 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 1 helix, 10 β-strands

ElementResiduesLengthSheet
β-strand22-2761
β-strand28-3032
β-strand31-3443
β-strand37-4043
β-strand45-5171
β-strand57-6371
β-strand69-7461
β-strand80-8452
β-strand93-9862
β-strand104-10962
α-helix117-12913

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Proteasomal ubiquitin receptor ADRM1Aprotein149Homo sapiensQ16186 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>5IRS_1 Proteasomal ubiquitin receptor ADRM1 (chains A)
TTSGALFPSLVPGSRGASNKYLVEFRAGKMSLKGTTVTPDKRKGLVYIQQTDDSLIHFCW
KDRTSGNVEDDLIIFPDDCEFKRVPQCPSGRVYVLKFKAGSKRLFFWMQEPKTDQDEEHC
RKVNEYLNNPPMPGALGASGSSGHELSAL

Ligands and cofactors

IDNameFormulaCopies
DTT2,3-dihydroxy-1,4-dithiobutaneC4 H10 O2 S22

Primary citation

Structures of Rpn1 T1:Rad23 and hRpn13:hPLIC2 Reveal Distinct Binding Mechanisms between Substrate Receptors and Shuttle Factors of the Proteasome. Chen, X., Randles, L., Shi, K. et al. Structure (2016) 24:1257-1270. DOI 10.1016/j.str.2016.05.018 · PubMed

Other PDB entries of the same protein (UniProt Q16186 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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