5vhp

Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle

Method: ELECTRON MICROSCOPY Dmax: 199.2 Å Quality: GOOD

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

26S proteasome non-ATPase regulatory subunit 10

Homo sapiens

UniProt O75832

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 G; UniProt 3–226 Not recorded 26S proteasome regulatory subunit 7 × 1 (P35998) 26S proteasome regulatory subunit 4 × 1 (P62191) 26S proteasome regulatory subunit 6B × 1 (P43686) 26S proteasome regulatory subunit 10B × 1 (P62333) 26S proteasome regulatory subunit 6A × 1 (P17980) 26S proteasome regulatory subunit 8 × 1 (P62195) 26S proteasome non-ATPase regulatory subunit 2 × 1 (Q13200) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.90 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.

18 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSD10_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain G; PDBConstruct 1–224; UniProt 3–226

26S proteasome regulatory subunit 7

Homo sapiens

UniProt P35998

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 A; UniProt 159–424 Not recorded 26S proteasome non-ATPase regulatory subunit 10 × 1 (O75832) 26S proteasome regulatory subunit 4 × 1 (P62191) 26S proteasome regulatory subunit 6B × 1 (P43686) 26S proteasome regulatory subunit 10B × 1 (P62333) 26S proteasome regulatory subunit 6A × 1 (P17980) 26S proteasome regulatory subunit 8 × 1 (P62195) 26S proteasome non-ATPase regulatory subunit 2 × 1 (Q13200) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.90 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.

130 other PDB entries and 130 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRS7_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–266; UniProt 159–424

26S proteasome regulatory subunit 4

Homo sapiens

UniProt P62191

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 B; UniProt 167–432 Not recorded 26S proteasome non-ATPase regulatory subunit 10 × 1 (O75832) 26S proteasome regulatory subunit 7 × 1 (P35998) 26S proteasome regulatory subunit 6B × 1 (P43686) 26S proteasome regulatory subunit 10B × 1 (P62333) 26S proteasome regulatory subunit 6A × 1 (P17980) 26S proteasome regulatory subunit 8 × 1 (P62195) 26S proteasome non-ATPase regulatory subunit 2 × 1 (Q13200) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.90 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.

130 other PDB entries and 130 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRS4_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–266; UniProt 167–432

26S proteasome regulatory subunit 6B

Homo sapiens

UniProt P43686

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 D; UniProt 114–375 Not recorded 26S proteasome non-ATPase regulatory subunit 10 × 1 (O75832) 26S proteasome regulatory subunit 7 × 1 (P35998) 26S proteasome regulatory subunit 4 × 1 (P62191) 26S proteasome regulatory subunit 10B × 1 (P62333) 26S proteasome regulatory subunit 6A × 1 (P17980) 26S proteasome regulatory subunit 8 × 1 (P62195) 26S proteasome non-ATPase regulatory subunit 2 × 1 (Q13200) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.90 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.

130 other PDB entries and 130 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRS6B_HUMAN
Isoform P43686-2
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–262; UniProt 114–375

26S proteasome regulatory subunit 10B

Homo sapiens

UniProt P62333

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 E; UniProt 128–389 Not recorded 26S proteasome non-ATPase regulatory subunit 10 × 1 (O75832) 26S proteasome regulatory subunit 7 × 1 (P35998) 26S proteasome regulatory subunit 4 × 1 (P62191) 26S proteasome regulatory subunit 6B × 1 (P43686) 26S proteasome regulatory subunit 6A × 1 (P17980) 26S proteasome regulatory subunit 8 × 1 (P62195) 26S proteasome non-ATPase regulatory subunit 2 × 1 (Q13200) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.90 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.

54 other PDB entries and 54 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRS10_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–262; UniProt 128–389

26S proteasome regulatory subunit 6A

Homo sapiens

UniProt P17980

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 F; UniProt 166–432 Not recorded 26S proteasome non-ATPase regulatory subunit 10 × 1 (O75832) 26S proteasome regulatory subunit 7 × 1 (P35998) 26S proteasome regulatory subunit 4 × 1 (P62191) 26S proteasome regulatory subunit 6B × 1 (P43686) 26S proteasome regulatory subunit 10B × 1 (P62333) 26S proteasome regulatory subunit 8 × 1 (P62195) 26S proteasome non-ATPase regulatory subunit 2 × 1 (Q13200) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.90 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.

129 other PDB entries and 129 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRS6A_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–267; UniProt 166–432

26S proteasome regulatory subunit 8

Homo sapiens

UniProt P62195

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 C; UniProt 130–395 Not recorded 26S proteasome non-ATPase regulatory subunit 10 × 1 (O75832) 26S proteasome regulatory subunit 7 × 1 (P35998) 26S proteasome regulatory subunit 4 × 1 (P62191) 26S proteasome regulatory subunit 6B × 1 (P43686) 26S proteasome regulatory subunit 10B × 1 (P62333) 26S proteasome regulatory subunit 6A × 1 (P17980) 26S proteasome non-ATPase regulatory subunit 2 × 1 (Q13200) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.90 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.

127 other PDB entries and 127 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRS8_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain C; PDBConstruct 1–266; UniProt 130–395

26S proteasome non-ATPase regulatory subunit 2

Homo sapiens

UniProt Q13200

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 f; UniProt 70–853 Not recorded 26S proteasome non-ATPase regulatory subunit 10 × 1 (O75832) 26S proteasome regulatory subunit 7 × 1 (P35998) 26S proteasome regulatory subunit 4 × 1 (P62191) 26S proteasome regulatory subunit 6B × 1 (P43686) 26S proteasome regulatory subunit 10B × 1 (P62333) 26S proteasome regulatory subunit 6A × 1 (P17980) 26S proteasome regulatory subunit 8 × 1 (P62195) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.90 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.

121 other PDB entries and 121 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSMD2_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain f; PDBConstruct 1–784; UniProt 70–853

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 5vhp

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5vhp
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5vhp
Deposition date deposition_date2017-04-13
Structure title titleConformational Landscape of the p28-Bound Human Proteasome Regulatory Particle
Keywords keywordsp28, 26S proteasome, regulatory particle, 19S, gankyrin, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier57.79
Radius of gyration Rg (electron density) rg_electron57.80
Forward intensity I(0) i0908884000.00
Molecular weight molecular_weight251660.0 kDa
Excluded volume excluded_volume315740 ų
Envelope volume envelope_volume545290 ų
Hydration-shell volume shell_volume81615 ų
Envelope diameter envelope_diameter185.8
Shell Rg shell_rg57.70
Envelope Rg envelope_rg54.53
Shape Rg shape_rg57.80
Total Rg total_rg57.79
Total atoms total_atoms17635
Residues n_residues2265
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 dmax199.2
Rg (real space) rg_real57.79
Rg uncertainty (real space) rg_real_error2.22
I(0) (real space) i0_real9.0890e+08
I(0) uncertainty (real space) i0_real_error1.9260e+07
Rg (reciprocal space) rg_reciprocal57.75
I(0) (reciprocal space) i0_reciprocal908800000.0000
Solution quality estimate total_estimate0.8173
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary73.8
Skewness Skewness skewness0.206
Kurtosis Kurtosis kurtosis-0.609
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha47660000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)