7nao

Human PA28-20S proteasome complex

Method: ELECTRON MICROSCOPY Dmax: 208.9 Å Quality: GOOD

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

Proteasome subunit alpha type-2

OrganismNot specified

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain A; UniProt 1–234 Chain O; UniProt 1–234 Not recorded Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) Proteasome activator complex subunit 2 × 4 (Q9UL46) Proteasome activator complex subunit 1 × 3 (Q06323) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–234; UniProt 1–234 Author chain O; PDBConstruct 1–234; UniProt 1–234

Proteasome subunit alpha type-4

OrganismNot specified

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain B; UniProt 1–261 Chain P; UniProt 1–261 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) Proteasome activator complex subunit 2 × 4 (Q9UL46) Proteasome activator complex subunit 1 × 3 (Q06323) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–261; UniProt 1–261 Author chain P; PDBConstruct 1–261; UniProt 1–261

Proteasome subunit alpha type-7

OrganismNot specified

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain C; UniProt 1–248 Chain Q; UniProt 1–248 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) Proteasome activator complex subunit 2 × 4 (Q9UL46) Proteasome activator complex subunit 1 × 3 (Q06323) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–248; UniProt 1–248 Author chain Q; PDBConstruct 1–248; UniProt 1–248

Proteasome subunit alpha type-5

OrganismNot specified

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain D; UniProt 1–241 Chain R; UniProt 1–241 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) Proteasome activator complex subunit 2 × 4 (Q9UL46) Proteasome activator complex subunit 1 × 3 (Q06323) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–241; UniProt 1–241 Author chain R; PDBConstruct 1–241; UniProt 1–241

Proteasome subunit alpha type-1

OrganismNot specified

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain E; UniProt 1–263 Chain S; UniProt 1–263 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) Proteasome activator complex subunit 2 × 4 (Q9UL46) Proteasome activator complex subunit 1 × 3 (Q06323) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

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 5
Chains and sequence ranges Author chain E; PDBConstruct 1–263; UniProt 1–263 Author chain S; PDBConstruct 1–263; UniProt 1–263

Proteasome subunit alpha type-3

OrganismNot specified

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain F; UniProt 1–255 Chain T; UniProt 1–255 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) Proteasome activator complex subunit 2 × 4 (Q9UL46) Proteasome activator complex subunit 1 × 3 (Q06323) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

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 6
Chains and sequence ranges Author chain F; PDBConstruct 1–255; UniProt 1–255 Author chain T; PDBConstruct 1–255; UniProt 1–255

Proteasome subunit alpha type-6

OrganismNot specified

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain G; UniProt 1–246 Chain U; UniProt 1–246 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) Proteasome activator complex subunit 2 × 4 (Q9UL46) Proteasome activator complex subunit 1 × 3 (Q06323) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

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 7
Chains and sequence ranges Author chain G; PDBConstruct 1–246; UniProt 1–246 Author chain U; PDBConstruct 1–246; UniProt 1–246

Proteasome subunit beta type-7

OrganismNot specified

UniProt Q99436

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain H; UniProt 1–277 Chain V; UniProt 1–277 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) Proteasome activator complex subunit 2 × 4 (Q9UL46) Proteasome activator complex subunit 1 × 3 (Q06323) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

159 other PDB entries and 160 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB7_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–277; UniProt 1–277 Author chain V; PDBConstruct 1–277; UniProt 1–277

Proteasome subunit beta type-3

OrganismNot specified

UniProt P49720

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain I; UniProt 1–205 Chain W; UniProt 1–205 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) Proteasome activator complex subunit 2 × 4 (Q9UL46) Proteasome activator complex subunit 1 × 3 (Q06323) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

150 other PDB entries and 151 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB3_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain I; PDBConstruct 1–205; UniProt 1–205 Author chain W; PDBConstruct 1–205; UniProt 1–205

Proteasome subunit beta type-2

OrganismNot specified

UniProt P49721

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain J; UniProt 1–201 Chain X; UniProt 1–201 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) Proteasome activator complex subunit 2 × 4 (Q9UL46) Proteasome activator complex subunit 1 × 3 (Q06323) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

149 other PDB entries and 150 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB2_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain J; PDBConstruct 1–201; UniProt 1–201 Author chain X; PDBConstruct 1–201; UniProt 1–201

Proteasome subunit beta type-5

OrganismNot specified

UniProt P28074

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain K; UniProt 1–263 Chain Y; UniProt 1–263 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) Proteasome activator complex subunit 2 × 4 (Q9UL46) Proteasome activator complex subunit 1 × 3 (Q06323) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

151 other PDB entries and 152 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB5_HUMAN
Isoform
PDB entities 11
Chains and sequence ranges Author chain K; PDBConstruct 1–263; UniProt 1–263 Author chain Y; PDBConstruct 1–263; UniProt 1–263

Proteasome subunit beta type-1

OrganismNot specified

UniProt P20618

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain L; UniProt 1–241 Chain Z; UniProt 1–241 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) Proteasome activator complex subunit 2 × 4 (Q9UL46) Proteasome activator complex subunit 1 × 3 (Q06323) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

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

View Construct and Data Evidence
UniProt name PSB1_HUMAN
Isoform
PDB entities 12
Chains and sequence ranges Author chain L; PDBConstruct 1–241; UniProt 1–241 Author chain Z; PDBConstruct 1–241; UniProt 1–241

Proteasome subunit beta type-4

OrganismNot specified

UniProt P28070

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain M; UniProt 1–264 Chain a; UniProt 1–264 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-6 × 2 (P28072) Proteasome activator complex subunit 2 × 4 (Q9UL46) Proteasome activator complex subunit 1 × 3 (Q06323) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

145 other PDB entries and 146 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB4_HUMAN
Isoform
PDB entities 13
Chains and sequence ranges Author chain M; PDBConstruct 1–264; UniProt 1–264 Author chain a; PDBConstruct 1–264; UniProt 1–264

Proteasome subunit beta type-6

OrganismNot specified

UniProt P28072

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain N; UniProt 1–239 Chain b; UniProt 1–239 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome activator complex subunit 2 × 4 (Q9UL46) Proteasome activator complex subunit 1 × 3 (Q06323) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

141 other PDB entries and 142 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB6_HUMAN
Isoform
PDB entities 14
Chains and sequence ranges Author chain N; PDBConstruct 1–239; UniProt 1–239 Author chain b; PDBConstruct 1–239; UniProt 1–239

Proteasome activator complex subunit 2

OrganismNot specified

UniProt Q9UL46

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain d; UniProt 1–239 Chain f; UniProt 1–239 Chain h; UniProt 1–239 Chain i; UniProt 1–239 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) Proteasome activator complex subunit 1 × 3 (Q06323) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

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

View Construct and Data Evidence
UniProt name PSME2_HUMAN
Isoform
PDB entities 15
Chains and sequence ranges Author chain d; PDBConstruct 1–239; UniProt 1–239 Author chain f; PDBConstruct 1–239; UniProt 1–239 Author chain h; PDBConstruct 1–239; UniProt 1–239 Author chain i; PDBConstruct 1–239; UniProt 1–239

Proteasome activator complex subunit 1

OrganismNot specified

UniProt Q06323

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 × 35 PDB declaration: 35-meric(35) Consistent with protein copy count Chain c; UniProt 1–249 Chain e; UniProt 1–249 Chain g; UniProt 1–249 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) Proteasome activator complex subunit 2 × 4 (Q9UL46) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.90 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSME1_HUMAN
Isoform
PDB entities 16
Chains and sequence ranges Author chain c; PDBConstruct 1–249; UniProt 1–249 Author chain e; PDBConstruct 1–249; UniProt 1–249 Author chain g; PDBConstruct 1–249; UniProt 1–249

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 7nao

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7nao
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7nao
Deposition date deposition_date2021-06-22
Structure title titleHuman PA28-20S proteasome complex
Keywords keywordsproteasome, 20S, PA28, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier69.63
Radius of gyration Rg (electron density) rg_electron70.04
Forward intensity I(0) i09038510000.00
Molecular weight molecular_weight825020.0 kDa
Excluded volume excluded_volume1040800 ų
Envelope volume envelope_volume1509700 ų
Hydration-shell volume shell_volume181790 ų
Envelope diameter envelope_diameter250.1
Shell Rg shell_rg70.55
Envelope Rg envelope_rg68.19
Shape Rg shape_rg70.07
Total Rg total_rg69.91
Total atoms total_atoms58083
Residues n_residues7741
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 dmax208.9
Rg (real space) rg_real69.26
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real8.9950e+09
I(0) uncertainty (real space) i0_real_error1.5250e+08
Rg (reciprocal space) rg_reciprocal68.84
I(0) (reciprocal space) i0_reciprocal9021000000.0000
Solution quality estimate total_estimate0.8498
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary76.0
Skewness Skewness skewness0.545
Kurtosis Kurtosis kurtosis-0.113
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0363
Highest regularization parameter α highest_alpha1111000000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.852; Stabil: 0.997; Sysdev: 1.000; Positv: 1.000; Valcen: 0.985; Smooth: 0.497

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

7. Fold Classification (SCOP + CATH) 10 domains

CATH v4.4 (10 domains)

Domain ID domain_id7naoA01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id7naoB01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id7naoC01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id7naoD01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id7naoH01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id7naoO01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id7naoP01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id7naoQ01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id7naoR01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id7naoV01
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

8. Citations (1)

9. Files and Curves (10)