6uth

Allosteric coupling between alpha-rings of 20S proteasome, 20S proteasome singly capped with a PA26/E102A_PANc, together with LFP incubation

Method: ELECTRON MICROSCOPY
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Proteasome subunit alpha

Thermoplasma acidophilum

UniProt P25156

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 35 Proteasome subunit beta × 14 (P28061) Proteasome activator protein PA26 × 7 (Q38BM8) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name PSA_THEAC
Isoform —
PDB entities 1, 3
Chains and sequence ranges Author chain A; PDBConstruct 1–227; UniProt 7–233 Author chain B; PDBConstruct 1–227; UniProt 7–233 Author chain C; PDBConstruct 1–227; UniProt 7–233 Author chain D; PDBConstruct 1–227; UniProt 7–233 Author chain E; PDBConstruct 1–227; UniProt 7–233 Author chain F; PDBConstruct 1–227; UniProt 7–233 Author chain G; PDBConstruct 1–227; UniProt 7–233 Author chain O; PDBConstruct 1–227; UniProt 7–233 Author chain P; PDBConstruct 1–227; UniProt 7–233 Author chain Q; PDBConstruct 1–227; UniProt 7–233 Author chain R; PDBConstruct 1–227; UniProt 7–233 Author chain S; PDBConstruct 1–227; UniProt 7–233 Author chain T; PDBConstruct 1–227; UniProt 7–233 Author chain U; PDBConstruct 1–227; UniProt 7–233

Proteasome subunit beta

Thermoplasma acidophilum

UniProt P28061

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 35 Proteasome subunit alpha × 7 (P25156) Proteasome subunit alpha × 7 (P25156) Proteasome activator protein PA26 × 7 (Q38BM8) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name PSB_THEAC
Isoform —
PDB entities 2
Chains and sequence ranges Author chain 1; PDBConstruct 1–203; UniProt 9–211 Author chain 2; PDBConstruct 1–203; UniProt 9–211 Author chain H; PDBConstruct 1–203; UniProt 9–211 Author chain I; PDBConstruct 1–203; UniProt 9–211 Author chain J; PDBConstruct 1–203; UniProt 9–211 Author chain K; PDBConstruct 1–203; UniProt 9–211 Author chain L; PDBConstruct 1–203; UniProt 9–211 Author chain M; PDBConstruct 1–203; UniProt 9–211 Author chain N; PDBConstruct 1–203; UniProt 9–211 Author chain V; PDBConstruct 1–203; UniProt 9–211 Author chain W; PDBConstruct 1–203; UniProt 9–211 Author chain X; PDBConstruct 1–203; UniProt 9–211 Author chain Y; PDBConstruct 1–203; UniProt 9–211 Author chain Z; PDBConstruct 1–203; UniProt 9–211

Proteasome activator protein PA26

Trypanosoma brucei brucei

UniProt Q38BM8

State in the Current Structure

Assembly Physical composition Protein state Molecular copy count Associated components Data consistency
1 Protein heterocomplex Heteromer Protein 35 Proteasome subunit alpha × 7 (P25156) Proteasome subunit beta × 14 (P28061) Proteasome subunit alpha × 7 (P25156) Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence
UniProt name Q38BM8_TRYB2
Isoform —
PDB entities 4
Chains and sequence ranges Author chain a; PDBConstruct 1–220; UniProt 4–223 Author chain b; PDBConstruct 1–220; UniProt 4–223 Author chain c; PDBConstruct 1–220; UniProt 4–223 Author chain d; PDBConstruct 1–220; UniProt 4–223 Author chain e; PDBConstruct 1–220; UniProt 4–223 Author chain f; PDBConstruct 1–220; UniProt 4–223 Author chain g; PDBConstruct 1–220; UniProt 4–223

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id6uth
Deposition date deposition_date2019-10-29
Structure title titleAllosteric coupling between alpha-rings of 20S proteasome, 20S proteasome singly capped with a PA26/E102A_PANc, together with LFP incubation
Keywords keywordsPA26PANc, proteasome, substrate LFP, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY
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3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

6uth__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

6uth__assembly_1__model_1 | I(q)

10-2 10-1 106 107 108 109 q (1/Angstrom) I(q)
100 plotted points; both axes use logarithmic scales.

6uth__assembly_1__model_1 | P(r) · Pending

The new assembly/model P(r) has not been calculated yet This placeholder does not display legacy data r (Angstrom) P(r)
P(r) will be calculated and displayed separately for the same assembly/model.
Rg(Guinier)70.15 Å
Rg (electron density)70.15 Å
Total Rg70.07 Å
Atom count58394
Residues7553
Excluded volume1048100 ų
Maximum q0.500 Å⁻¹
Assembly Model Structure unit Oligomeric description Status CRYSOL Actions
1 1 6uth__assembly_1__model_1 35-meric (35) Success 4.1.3-1-20251215 (887e7ef) View Download
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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (4)

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7. Citations (1)