9qon

Ternary complex of the human 20S proteasome in complex with Importin-9 and two homodimers of Akirin-2 - focussed refinement on the alpha subunits, Ipo-9 and Ak2

Method: ELECTRON MICROSCOPY Dmax: 132.1 Å Quality: EXCELLENT

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

Importin-9

Homo sapiens

UniProt Q96P70

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain A; UniProt 1–1041 Not recorded Akirin-2 × 3 (Q53H80) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome subunit alpha type-2 × 1 (P25787) Proteasome subunit alpha type-4 × 1 (P25789) Proteasome subunit alpha type-7 × 1 (O14818) Proteasome subunit alpha type-5 × 1 (P28066) Proteasome subunit alpha type-1 × 1 (P25786) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

6 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IPO9_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1041; UniProt 1–1041

Akirin-2

Homo sapiens

UniProt Q53H80

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain B; UniProt 1–203 Chain C; UniProt 1–203 Chain D; UniProt 1–203 Not recorded Importin-9 × 1 (Q96P70) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome subunit alpha type-2 × 1 (P25787) Proteasome subunit alpha type-4 × 1 (P25789) Proteasome subunit alpha type-7 × 1 (O14818) Proteasome subunit alpha type-5 × 1 (P28066) Proteasome subunit alpha type-1 × 1 (P25786) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name AKIR2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–203; UniProt 1–203 Author chain C; PDBConstruct 1–203; UniProt 1–203 Author chain D; PDBConstruct 1–203; UniProt 1–203

Proteasome subunit alpha type-3

Homo sapiens

UniProt P25788

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain F; UniProt 1–255 Not recorded Importin-9 × 1 (Q96P70) Akirin-2 × 3 (Q53H80) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome subunit alpha type-2 × 1 (P25787) Proteasome subunit alpha type-4 × 1 (P25789) Proteasome subunit alpha type-7 × 1 (O14818) Proteasome subunit alpha type-5 × 1 (P28066) Proteasome subunit alpha type-1 × 1 (P25786) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

172 other PDB entries and 175 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA3_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain F; PDBConstruct 1–255; UniProt 1–255

Proteasome subunit alpha type-6

Homo sapiens

UniProt P60900

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain G; UniProt 1–246 Not recorded Importin-9 × 1 (Q96P70) Akirin-2 × 3 (Q53H80) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-2 × 1 (P25787) Proteasome subunit alpha type-4 × 1 (P25789) Proteasome subunit alpha type-7 × 1 (O14818) Proteasome subunit alpha type-5 × 1 (P28066) Proteasome subunit alpha type-1 × 1 (P25786) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

170 other PDB entries and 171 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA6_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain G; PDBConstruct 1–246; UniProt 1–246

Proteasome subunit alpha type-2

Homo sapiens

UniProt P25787

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain O; UniProt 1–234 Not recorded Importin-9 × 1 (Q96P70) Akirin-2 × 3 (Q53H80) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome subunit alpha type-4 × 1 (P25789) Proteasome subunit alpha type-7 × 1 (O14818) Proteasome subunit alpha type-5 × 1 (P28066) Proteasome subunit alpha type-1 × 1 (P25786) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

170 other PDB entries and 171 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA2_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain O; PDBConstruct 1–234; UniProt 1–234

Proteasome subunit alpha type-4

Homo sapiens

UniProt P25789

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain P; UniProt 1–261 Not recorded Importin-9 × 1 (Q96P70) Akirin-2 × 3 (Q53H80) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome subunit alpha type-2 × 1 (P25787) Proteasome subunit alpha type-7 × 1 (O14818) Proteasome subunit alpha type-5 × 1 (P28066) Proteasome subunit alpha type-1 × 1 (P25786) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

170 other PDB entries and 171 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA4_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain P; PDBConstruct 1–261; UniProt 1–261

Proteasome subunit alpha type-7

Homo sapiens

UniProt O14818

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain Q; UniProt 1–248 Not recorded Importin-9 × 1 (Q96P70) Akirin-2 × 3 (Q53H80) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome subunit alpha type-2 × 1 (P25787) Proteasome subunit alpha type-4 × 1 (P25789) Proteasome subunit alpha type-5 × 1 (P28066) Proteasome subunit alpha type-1 × 1 (P25786) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

170 other PDB entries and 171 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA7_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain Q; PDBConstruct 1–248; UniProt 1–248

Proteasome subunit alpha type-5

Homo sapiens

UniProt P28066

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain R; UniProt 1–241 Not recorded Importin-9 × 1 (Q96P70) Akirin-2 × 3 (Q53H80) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome subunit alpha type-2 × 1 (P25787) Proteasome subunit alpha type-4 × 1 (P25789) Proteasome subunit alpha type-7 × 1 (O14818) Proteasome subunit alpha type-1 × 1 (P25786) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

170 other PDB entries and 171 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA5_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain R; PDBConstruct 1–241; UniProt 1–241

Proteasome subunit alpha type-1

Homo sapiens

UniProt P25786

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 × 11 PDB declaration: 11-meric(11) Consistent with protein copy count Chain S; UniProt 1–263 Not recorded Importin-9 × 1 (Q96P70) Akirin-2 × 3 (Q53H80) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome subunit alpha type-2 × 1 (P25787) Proteasome subunit alpha type-4 × 1 (P25789) Proteasome subunit alpha type-7 × 1 (O14818) Proteasome subunit alpha type-5 × 1 (P28066) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 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.

170 other PDB entries and 171 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA1_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain S; PDBConstruct 1–263; UniProt 1–263

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 9qon

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9qon
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9qon
Deposition date deposition_date2025-03-26
Structure title titleTernary complex of the human 20S proteasome in complex with Importin-9 and two homodimers of Akirin-2 - focussed refinement on the alpha subunits, Ipo-9 and Ak2
Keywords keywords20S proteasome, 20S, proteasome, nuclear iport, akirin, akirin2, importin 9, importin, PROTEIN TRANSPORT; PROTEIN TRANSPORT
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier42.59
Radius of gyration Rg (electron density) rg_electron41.98
Forward intensity I(0) i0816007000.00
Molecular weight molecular_weight235250.0 kDa
Excluded volume excluded_volume294420 ų
Envelope volume envelope_volume407190 ų
Hydration-shell volume shell_volume77113 ų
Envelope diameter envelope_diameter142.2
Shell Rg shell_rg50.25
Envelope Rg envelope_rg41.74
Shape Rg shape_rg41.96
Total Rg total_rg42.41
Total atoms total_atoms32930
Residues n_residues2120
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 dmax132.1
Rg (real space) rg_real42.36
Rg uncertainty (real space) rg_real_error1.18
I(0) (real space) i0_real8.1600e+08
I(0) uncertainty (real space) i0_real_error1.6660e+07
Rg (reciprocal space) rg_reciprocal42.59
I(0) (reciprocal space) i0_reciprocal816200000.0000
Solution quality estimate total_estimate0.9028
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.5
Skewness Skewness skewness0.086
Kurtosis Kurtosis kurtosis-0.595
Angular range angular_range— – 0.1850 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha106700000.0000
Real-space data points n_real_points38
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.942; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.931

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

8. Citations (1)

9. Files and Curves (10)