3jck

Structure of the yeast 26S proteasome lid sub-complex

Method: ELECTRON MICROSCOPY Dmax: 188.9 Å Quality: GOOD

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

26S proteasome regulatory subunit RPN3

Saccharomyces cerevisiae S288c

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 131–523 Not recorded 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 RPN8 × 1 (Q08723) 26S proteasome regulatory subunit RPN9 × 1 (Q04062) Ubiquitin carboxyl-terminal hydrolase RPN11 × 1 (P43588) 26S proteasome regulatory subunit RPN12 × 1 (P32496) 26S proteasome complex subunit SEM1 × 1 (O94742) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP;pH 7.5;50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP cryo-EM vitrification conditions:4 uL sample was applied to the grid, blotted for 2 seconds, and plunged into liquid ethane.;85 K;Cryogen ETHANE;4 uL sample was applied to the grid, blotted for 2 seconds at 4 degrees C, and plunged into liquid ethane using a manual plunger. Resolution 3.50 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 1
Chains and sequence ranges Author chain A; PDBConstruct 46–438; UniProt 131–523

26S proteasome regulatory subunit RPN5

Saccharomyces cerevisiae S288c

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain B; UniProt 1–445 Not recorded 26S proteasome regulatory subunit RPN3 × 1 (P40016) 26S proteasome regulatory subunit RPN6 × 1 (Q12377) 26S proteasome regulatory subunit RPN7 × 1 (Q06103) 26S proteasome regulatory subunit RPN8 × 1 (Q08723) 26S proteasome regulatory subunit RPN9 × 1 (Q04062) Ubiquitin carboxyl-terminal hydrolase RPN11 × 1 (P43588) 26S proteasome regulatory subunit RPN12 × 1 (P32496) 26S proteasome complex subunit SEM1 × 1 (O94742) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP;pH 7.5;50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP cryo-EM vitrification conditions:4 uL sample was applied to the grid, blotted for 2 seconds, and plunged into liquid ethane.;85 K;Cryogen ETHANE;4 uL sample was applied to the grid, blotted for 2 seconds at 4 degrees C, and plunged into liquid ethane using a manual plunger. Resolution 3.50 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–445; UniProt 1–445

26S proteasome regulatory subunit RPN6

Saccharomyces cerevisiae S288c

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain C; UniProt 1–434 Not recorded 26S proteasome regulatory subunit RPN3 × 1 (P40016) 26S proteasome regulatory subunit RPN5 × 1 (Q12250) 26S proteasome regulatory subunit RPN7 × 1 (Q06103) 26S proteasome regulatory subunit RPN8 × 1 (Q08723) 26S proteasome regulatory subunit RPN9 × 1 (Q04062) Ubiquitin carboxyl-terminal hydrolase RPN11 × 1 (P43588) 26S proteasome regulatory subunit RPN12 × 1 (P32496) 26S proteasome complex subunit SEM1 × 1 (O94742) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP;pH 7.5;50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP cryo-EM vitrification conditions:4 uL sample was applied to the grid, blotted for 2 seconds, and plunged into liquid ethane.;85 K;Cryogen ETHANE;4 uL sample was applied to the grid, blotted for 2 seconds at 4 degrees C, and plunged into liquid ethane using a manual plunger. Resolution 3.50 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–434; UniProt 1–434

26S proteasome regulatory subunit RPN7

Saccharomyces cerevisiae S288c

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain D; UniProt 1–429 Not recorded 26S proteasome regulatory subunit RPN3 × 1 (P40016) 26S proteasome regulatory subunit RPN5 × 1 (Q12250) 26S proteasome regulatory subunit RPN6 × 1 (Q12377) 26S proteasome regulatory subunit RPN8 × 1 (Q08723) 26S proteasome regulatory subunit RPN9 × 1 (Q04062) Ubiquitin carboxyl-terminal hydrolase RPN11 × 1 (P43588) 26S proteasome regulatory subunit RPN12 × 1 (P32496) 26S proteasome complex subunit SEM1 × 1 (O94742) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP;pH 7.5;50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP cryo-EM vitrification conditions:4 uL sample was applied to the grid, blotted for 2 seconds, and plunged into liquid ethane.;85 K;Cryogen ETHANE;4 uL sample was applied to the grid, blotted for 2 seconds at 4 degrees C, and plunged into liquid ethane using a manual plunger. Resolution 3.50 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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–429; UniProt 1–429

26S proteasome regulatory subunit RPN8

Saccharomyces cerevisiae S288c

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain E; UniProt 1–338 Not recorded 26S proteasome regulatory subunit RPN3 × 1 (P40016) 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 RPN9 × 1 (Q04062) Ubiquitin carboxyl-terminal hydrolase RPN11 × 1 (P43588) 26S proteasome regulatory subunit RPN12 × 1 (P32496) 26S proteasome complex subunit SEM1 × 1 (O94742) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP;pH 7.5;50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP cryo-EM vitrification conditions:4 uL sample was applied to the grid, blotted for 2 seconds, and plunged into liquid ethane.;85 K;Cryogen ETHANE;4 uL sample was applied to the grid, blotted for 2 seconds at 4 degrees C, and plunged into liquid ethane using a manual plunger. Resolution 3.50 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 5
Chains and sequence ranges Author chain E; PDBConstruct 1–338; UniProt 1–338

26S proteasome regulatory subunit RPN9

Saccharomyces cerevisiae S288c

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain F; UniProt 1–393 Not recorded 26S proteasome regulatory subunit RPN3 × 1 (P40016) 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 RPN8 × 1 (Q08723) Ubiquitin carboxyl-terminal hydrolase RPN11 × 1 (P43588) 26S proteasome regulatory subunit RPN12 × 1 (P32496) 26S proteasome complex subunit SEM1 × 1 (O94742) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP;pH 7.5;50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP cryo-EM vitrification conditions:4 uL sample was applied to the grid, blotted for 2 seconds, and plunged into liquid ethane.;85 K;Cryogen ETHANE;4 uL sample was applied to the grid, blotted for 2 seconds at 4 degrees C, and plunged into liquid ethane using a manual plunger. Resolution 3.50 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 6
Chains and sequence ranges Author chain F; PDBConstruct 1–393; UniProt 1–393

Ubiquitin carboxyl-terminal hydrolase RPN11

Saccharomyces cerevisiae S288c

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain G; UniProt 1–306 Not recorded 26S proteasome regulatory subunit RPN3 × 1 (P40016) 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 RPN8 × 1 (Q08723) 26S proteasome regulatory subunit RPN9 × 1 (Q04062) 26S proteasome regulatory subunit RPN12 × 1 (P32496) 26S proteasome complex subunit SEM1 × 1 (O94742) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP;pH 7.5;50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP cryo-EM vitrification conditions:4 uL sample was applied to the grid, blotted for 2 seconds, and plunged into liquid ethane.;85 K;Cryogen ETHANE;4 uL sample was applied to the grid, blotted for 2 seconds at 4 degrees C, and plunged into liquid ethane using a manual plunger. Resolution 3.50 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 7
Chains and sequence ranges Author chain G; PDBConstruct 1–306; UniProt 1–306

26S proteasome regulatory subunit RPN12

Saccharomyces cerevisiae S288c

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain H; UniProt 1–274 Not recorded 26S proteasome regulatory subunit RPN3 × 1 (P40016) 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 RPN8 × 1 (Q08723) 26S proteasome regulatory subunit RPN9 × 1 (Q04062) Ubiquitin carboxyl-terminal hydrolase RPN11 × 1 (P43588) 26S proteasome complex subunit SEM1 × 1 (O94742) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP;pH 7.5;50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP cryo-EM vitrification conditions:4 uL sample was applied to the grid, blotted for 2 seconds, and plunged into liquid ethane.;85 K;Cryogen ETHANE;4 uL sample was applied to the grid, blotted for 2 seconds at 4 degrees C, and plunged into liquid ethane using a manual plunger. Resolution 3.50 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 H; PDBConstruct 1–274; UniProt 1–274

26S proteasome complex subunit SEM1

Saccharomyces cerevisiae S288c

UniProt O94742

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain I; UniProt 1–89 Not recorded 26S proteasome regulatory subunit RPN3 × 1 (P40016) 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 RPN8 × 1 (Q08723) 26S proteasome regulatory subunit RPN9 × 1 (Q04062) Ubiquitin carboxyl-terminal hydrolase RPN11 × 1 (P43588) 26S proteasome regulatory subunit RPN12 × 1 (P32496) ZN ZINC ION × 1 ELECTRON MICROSCOPY cryo-EM buffer:50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP;pH 7.5;50 mM HEPES, 100 mM NaCl, 100 mM KCl, 1 mM TCEP cryo-EM vitrification conditions:4 uL sample was applied to the grid, blotted for 2 seconds, and plunged into liquid ethane.;85 K;Cryogen ETHANE;4 uL sample was applied to the grid, blotted for 2 seconds at 4 degrees C, and plunged into liquid ethane using a manual plunger. Resolution 3.50 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.

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

View Construct and Data Evidence
UniProt name SEM1_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain I; PDBConstruct 1–89; UniProt 1–89

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 3jck

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3jck
Deposition date deposition_date2015-12-20
Structure title titleStructure of the yeast 26S proteasome lid sub-complex
Keywords keywordsProteasome, deubiquitinase, Rpn11, protein homeostasis, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.74
Radius of gyration Rg (electron density) rg_electron55.99
Forward intensity I(0) i032656600000.00
Molecular weight molecular_weight1594000.0 kDa
Excluded volume excluded_volume2014700 ų
Envelope volume envelope_volume653090 ų
Hydration-shell volume shell_volume97574 ų
Envelope diameter envelope_diameter203.9
Shell Rg shell_rg57.21
Envelope Rg envelope_rg56.31
Shape Rg shape_rg55.99
Total Rg total_rg56.00
Total atoms total_atoms112280
Residues n_residues13885
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 dmax188.9
Rg (real space) rg_real55.87
Rg uncertainty (real space) rg_real_error2.40
I(0) (real space) i0_real3.2660e+10
I(0) uncertainty (real space) i0_real_error7.1720e+08
Rg (reciprocal space) rg_reciprocal55.62
I(0) (reciprocal space) i0_reciprocal32640000000.0000
Solution quality estimate total_estimate0.8648
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary60.7
Skewness Skewness skewness0.401
Kurtosis Kurtosis kurtosis-0.274
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha93690000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.865; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.645

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (11)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id3jckC00
Class class1 — Mainly Alpha
Architecture architecture25 — Alpha Horseshoe
Topology topology40 — Serine Threonine Protein Phosphatase 5, Tetratricopeptide repeat
Homologous superfamily homologous superfamily570
Domain ID domain_id3jckE01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology140 — Cytidine Deaminase; domain 2
Homologous superfamily homologous superfamily10 — Cytidine Deaminase, domain 2

8. Citations (1)

9. Files and Curves (10)