3j47

Formation of an intricate helical bundle dictates the assembly of the 26S proteasome lid

Method: ELECTRON MICROSCOPY Dmax: 95.8 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

26S proteasome regulatory subunit RPN11

OrganismNot specified

UniProt P43588

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain V; UniProt 230–298 Fragment:last three C-terminal helices (UNP residues 230-298) 26S proteasome regulatory subunit RPN8 × 1 (Q08723) 26S proteasome regulatory subunit RPN9 × 1 (Q04062) 26S proteasome regulatory subunit RPN5 × 1 (Q12250) 26S proteasome regulatory subunit RPN6 × 1 (Q12377) 26S proteasome regulatory subunit RPN7 × 1 (Q06103) 26S proteasome regulatory subunit RPN3 × 1 (P40016) 26S proteasome regulatory subunit RPN12 × 1 (P32496) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

37 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPN11_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain V; PDBConstruct 1–69; UniProt 230–298

26S proteasome regulatory subunit RPN8

OrganismNot specified

UniProt Q08723

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain U; UniProt 188–308 Fragment:last three C-terminal helices (UNP residues 188-308) 26S proteasome regulatory subunit RPN11 × 1 (P43588) 26S proteasome regulatory subunit RPN9 × 1 (Q04062) 26S proteasome regulatory subunit RPN5 × 1 (Q12250) 26S proteasome regulatory subunit RPN6 × 1 (Q12377) 26S proteasome regulatory subunit RPN7 × 1 (Q06103) 26S proteasome regulatory subunit RPN3 × 1 (P40016) 26S proteasome regulatory subunit RPN12 × 1 (P32496) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

37 other PDB entries and 42 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPN8_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain U; PDBConstruct 1–121; UniProt 188–308

26S proteasome regulatory subunit RPN9

OrganismNot specified

UniProt Q04062

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain O; UniProt 360–387 Fragment:C-terminal helix (UNP residues 360-387) 26S proteasome regulatory subunit RPN11 × 1 (P43588) 26S proteasome regulatory subunit RPN8 × 1 (Q08723) 26S proteasome regulatory subunit RPN5 × 1 (Q12250) 26S proteasome regulatory subunit RPN6 × 1 (Q12377) 26S proteasome regulatory subunit RPN7 × 1 (Q06103) 26S proteasome regulatory subunit RPN3 × 1 (P40016) 26S proteasome regulatory subunit RPN12 × 1 (P32496) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

32 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPN9_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain O; PDBConstruct 1–28; UniProt 360–387

26S proteasome regulatory subunit RPN5

OrganismNot specified

UniProt Q12250

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain P; UniProt 409–442 Fragment:C-terminal helix (UNP residues 409-442) 26S proteasome regulatory subunit RPN11 × 1 (P43588) 26S proteasome regulatory subunit RPN8 × 1 (Q08723) 26S proteasome regulatory subunit RPN9 × 1 (Q04062) 26S proteasome regulatory subunit RPN6 × 1 (Q12377) 26S proteasome regulatory subunit RPN7 × 1 (Q06103) 26S proteasome regulatory subunit RPN3 × 1 (P40016) 26S proteasome regulatory subunit RPN12 × 1 (P32496) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

29 other PDB entries and 30 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPN5_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain P; PDBConstruct 1–34; UniProt 409–442

26S proteasome regulatory subunit RPN6

OrganismNot specified

UniProt Q12377

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain Q; UniProt 407–431 Fragment:C-terminal helix (UNP residues 407-431) 26S proteasome regulatory subunit RPN11 × 1 (P43588) 26S proteasome regulatory subunit RPN8 × 1 (Q08723) 26S proteasome regulatory subunit RPN9 × 1 (Q04062) 26S proteasome regulatory subunit RPN5 × 1 (Q12250) 26S proteasome regulatory subunit RPN7 × 1 (Q06103) 26S proteasome regulatory subunit RPN3 × 1 (P40016) 26S proteasome regulatory subunit RPN12 × 1 (P32496) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

28 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPN6_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain Q; PDBConstruct 1–25; UniProt 407–431

26S proteasome regulatory subunit RPN7

OrganismNot specified

UniProt Q06103

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain R; UniProt 397–422 Fragment:C-terminal helix (UNP residues 397-422) 26S proteasome regulatory subunit RPN11 × 1 (P43588) 26S proteasome regulatory subunit RPN8 × 1 (Q08723) 26S proteasome regulatory subunit RPN9 × 1 (Q04062) 26S proteasome regulatory subunit RPN5 × 1 (Q12250) 26S proteasome regulatory subunit RPN6 × 1 (Q12377) 26S proteasome regulatory subunit RPN3 × 1 (P40016) 26S proteasome regulatory subunit RPN12 × 1 (P32496) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

28 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPN7_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain R; PDBConstruct 1–26; UniProt 397–422

26S proteasome regulatory subunit RPN3

OrganismNot specified

UniProt P40016

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain S; UniProt 455–478 Fragment:C-terminal helix (UNP residues 455-478) 26S proteasome regulatory subunit RPN11 × 1 (P43588) 26S proteasome regulatory subunit RPN8 × 1 (Q08723) 26S proteasome regulatory subunit RPN9 × 1 (Q04062) 26S proteasome regulatory subunit RPN5 × 1 (Q12250) 26S proteasome regulatory subunit RPN6 × 1 (Q12377) 26S proteasome regulatory subunit RPN7 × 1 (Q06103) 26S proteasome regulatory subunit RPN12 × 1 (P32496) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

28 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPN3_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain S; PDBConstruct 1–24; UniProt 455–478

26S proteasome regulatory subunit RPN12

OrganismNot specified

UniProt P32496

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain T; UniProt 256–272 Fragment:C-terminal helix (UNP residues 256-272) 26S proteasome regulatory subunit RPN11 × 1 (P43588) 26S proteasome regulatory subunit RPN8 × 1 (Q08723) 26S proteasome regulatory subunit RPN9 × 1 (Q04062) 26S proteasome regulatory subunit RPN5 × 1 (Q12250) 26S proteasome regulatory subunit RPN6 × 1 (Q12377) 26S proteasome regulatory subunit RPN7 × 1 (Q06103) 26S proteasome regulatory subunit RPN3 × 1 (P40016) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.40 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

28 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RPN12_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain T; PDBConstruct 1–17; UniProt 256–272

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.

SAXS scattering curve SAXS Profile

SAXS profile for 3j47

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3j47
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3j47
Deposition date deposition_date2013-06-27
Structure title titleFormation of an intricate helical bundle dictates the assembly of the 26S proteasome lid
Keywords keywordsalpha helix bundle, hybrid method, flexible fitting, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier24.66
Radius of gyration Rg (electron density) rg_electron24.61
Forward intensity I(0) i021210300.00
Molecular weight molecular_weight35525.0 kDa
Excluded volume excluded_volume44769 ų
Envelope volume envelope_volume55038 ų
Hydration-shell volume shell_volume20524 ų
Envelope diameter envelope_diameter96.9
Shell Rg shell_rg29.04
Envelope Rg envelope_rg25.17
Shape Rg shape_rg24.60
Total Rg total_rg25.20
Total atoms total_atoms2498
Residues n_residues308
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax95.8
Rg (real space) rg_real25.03
Rg uncertainty (real space) rg_real_error0.92
I(0) (real space) i0_real2.1210e+07
I(0) uncertainty (real space) i0_real_error3.2960e+05
Rg (reciprocal space) rg_reciprocal24.94
I(0) (reciprocal space) i0_reciprocal21210000.0000
Solution quality estimate total_estimate0.7252
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.8
Skewness Skewness skewness0.662
Kurtosis Kurtosis kurtosis-0.018
Angular range angular_range— – 0.3200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5792000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.402; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.238; Smooth: 0.978

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (2)

9. Files and Curves (10)