8qz9

Human 20S proteasome assembly intermediate structure 4

Method: ELECTRON MICROSCOPY Dmax: 148.6 Å Quality: GOOD

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

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain A; UniProt 1–234 Not recorded 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) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome maturation protein × 1 (Q9Y244) Proteasome assembly chaperone 1 × 1 (O95456) Proteasome assembly chaperone 2 × 1 (Q969U7) Proteasome subunit beta type-7 × 1 (Q99436) Proteasome subunit beta type-3 × 1 (P49720) Proteasome subunit beta type-2 × 1 (P49721) Proteasome subunit beta type-5 × 1 (P28074) Proteasome subunit beta type-1 × 1 (P20618) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.95 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

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain B; UniProt 1–261 Not recorded 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) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome maturation protein × 1 (Q9Y244) Proteasome assembly chaperone 1 × 1 (O95456) Proteasome assembly chaperone 2 × 1 (Q969U7) Proteasome subunit beta type-7 × 1 (Q99436) Proteasome subunit beta type-3 × 1 (P49720) Proteasome subunit beta type-2 × 1 (P49721) Proteasome subunit beta type-5 × 1 (P28074) Proteasome subunit beta type-1 × 1 (P20618) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.95 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

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain C; UniProt 1–248 Not recorded 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) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome maturation protein × 1 (Q9Y244) Proteasome assembly chaperone 1 × 1 (O95456) Proteasome assembly chaperone 2 × 1 (Q969U7) Proteasome subunit beta type-7 × 1 (Q99436) Proteasome subunit beta type-3 × 1 (P49720) Proteasome subunit beta type-2 × 1 (P49721) Proteasome subunit beta type-5 × 1 (P28074) Proteasome subunit beta type-1 × 1 (P20618) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.95 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

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain D; UniProt 1–241 Non-standard monomer:Yes (specific site not provided by mmCIF) 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) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome maturation protein × 1 (Q9Y244) Proteasome assembly chaperone 1 × 1 (O95456) Proteasome assembly chaperone 2 × 1 (Q969U7) Proteasome subunit beta type-7 × 1 (Q99436) Proteasome subunit beta type-3 × 1 (P49720) Proteasome subunit beta type-2 × 1 (P49721) Proteasome subunit beta type-5 × 1 (P28074) Proteasome subunit beta type-1 × 1 (P20618) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.95 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 2–242; 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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain E; UniProt 1–263 Non-standard monomer:Yes (specific site not provided by mmCIF) 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-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome maturation protein × 1 (Q9Y244) Proteasome assembly chaperone 1 × 1 (O95456) Proteasome assembly chaperone 2 × 1 (Q969U7) Proteasome subunit beta type-7 × 1 (Q99436) Proteasome subunit beta type-3 × 1 (P49720) Proteasome subunit beta type-2 × 1 (P49721) Proteasome subunit beta type-5 × 1 (P28074) Proteasome subunit beta type-1 × 1 (P20618) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.95 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 2–264; UniProt 1–263

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain F; UniProt 1–255 Not recorded 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) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome maturation protein × 1 (Q9Y244) Proteasome assembly chaperone 1 × 1 (O95456) Proteasome assembly chaperone 2 × 1 (Q969U7) Proteasome subunit beta type-7 × 1 (Q99436) Proteasome subunit beta type-3 × 1 (P49720) Proteasome subunit beta type-2 × 1 (P49721) Proteasome subunit beta type-5 × 1 (P28074) Proteasome subunit beta type-1 × 1 (P20618) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.95 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

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain G; UniProt 1–246 Non-standard monomer:Yes (specific site not provided by mmCIF) 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) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome maturation protein × 1 (Q9Y244) Proteasome assembly chaperone 1 × 1 (O95456) Proteasome assembly chaperone 2 × 1 (Q969U7) Proteasome subunit beta type-7 × 1 (Q99436) Proteasome subunit beta type-3 × 1 (P49720) Proteasome subunit beta type-2 × 1 (P49721) Proteasome subunit beta type-5 × 1 (P28074) Proteasome subunit beta type-1 × 1 (P20618) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.95 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 2–247; UniProt 1–246

Proteasome maturation protein

Homo sapiens

UniProt Q9Y244

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain H; UniProt 1–141 Not recorded 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) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome assembly chaperone 1 × 1 (O95456) Proteasome assembly chaperone 2 × 1 (Q969U7) Proteasome subunit beta type-7 × 1 (Q99436) Proteasome subunit beta type-3 × 1 (P49720) Proteasome subunit beta type-2 × 1 (P49721) Proteasome subunit beta type-5 × 1 (P28074) Proteasome subunit beta type-1 × 1 (P20618) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.95 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POMP_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–141; UniProt 1–141

Proteasome assembly chaperone 1

Homo sapiens

UniProt O95456

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain I; UniProt 1–288 Not recorded 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) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome maturation protein × 1 (Q9Y244) Proteasome assembly chaperone 2 × 1 (Q969U7) Proteasome subunit beta type-7 × 1 (Q99436) Proteasome subunit beta type-3 × 1 (P49720) Proteasome subunit beta type-2 × 1 (P49721) Proteasome subunit beta type-5 × 1 (P28074) Proteasome subunit beta type-1 × 1 (P20618) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.95 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSMG1_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain I; PDBConstruct 1–288; UniProt 1–288

Proteasome assembly chaperone 2

Homo sapiens

UniProt Q969U7

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain J; UniProt 1–264 Non-standard monomer:Yes (specific site not provided by mmCIF) 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) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome maturation protein × 1 (Q9Y244) Proteasome assembly chaperone 1 × 1 (O95456) Proteasome subunit beta type-7 × 1 (Q99436) Proteasome subunit beta type-3 × 1 (P49720) Proteasome subunit beta type-2 × 1 (P49721) Proteasome subunit beta type-5 × 1 (P28074) Proteasome subunit beta type-1 × 1 (P20618) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.95 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.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSMG2_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain J; PDBConstruct 2–265; UniProt 1–264

Proteasome subunit beta type-7

Homo sapiens

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain K; UniProt 1–277 Not recorded 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) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome maturation protein × 1 (Q9Y244) Proteasome assembly chaperone 1 × 1 (O95456) Proteasome assembly chaperone 2 × 1 (Q969U7) Proteasome subunit beta type-3 × 1 (P49720) Proteasome subunit beta type-2 × 1 (P49721) Proteasome subunit beta type-5 × 1 (P28074) Proteasome subunit beta type-1 × 1 (P20618) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.95 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 11
Chains and sequence ranges Author chain K; PDBConstruct 1–277; UniProt 1–277

Proteasome subunit beta type-3

Homo sapiens

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain L; UniProt 1–205 Not recorded 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) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome maturation protein × 1 (Q9Y244) Proteasome assembly chaperone 1 × 1 (O95456) Proteasome assembly chaperone 2 × 1 (Q969U7) Proteasome subunit beta type-7 × 1 (Q99436) Proteasome subunit beta type-2 × 1 (P49721) Proteasome subunit beta type-5 × 1 (P28074) Proteasome subunit beta type-1 × 1 (P20618) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.95 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 12
Chains and sequence ranges Author chain L; PDBConstruct 1–205; UniProt 1–205

Proteasome subunit beta type-2

Homo sapiens

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain M; UniProt 1–201 Non-standard monomer:Yes (specific site not provided by mmCIF) 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) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome maturation protein × 1 (Q9Y244) Proteasome assembly chaperone 1 × 1 (O95456) Proteasome assembly chaperone 2 × 1 (Q969U7) Proteasome subunit beta type-7 × 1 (Q99436) Proteasome subunit beta type-3 × 1 (P49720) Proteasome subunit beta type-5 × 1 (P28074) Proteasome subunit beta type-1 × 1 (P20618) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.95 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 13
Chains and sequence ranges Author chain M; PDBConstruct 2–202; UniProt 1–201

Proteasome subunit beta type-5

Homo sapiens

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain N; UniProt 1–263 Not recorded 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) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome maturation protein × 1 (Q9Y244) Proteasome assembly chaperone 1 × 1 (O95456) Proteasome assembly chaperone 2 × 1 (Q969U7) Proteasome subunit beta type-7 × 1 (Q99436) Proteasome subunit beta type-3 × 1 (P49720) Proteasome subunit beta type-2 × 1 (P49721) Proteasome subunit beta type-1 × 1 (P20618) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.95 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 14
Chains and sequence ranges Author chain N; PDBConstruct 1–263; UniProt 1–263

Proteasome subunit beta type-1

Homo sapiens

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain O; UniProt 1–241 Not recorded 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) Proteasome subunit alpha type-3 × 1 (P25788) Proteasome subunit alpha type-6 × 1 (P60900) Proteasome maturation protein × 1 (Q9Y244) Proteasome assembly chaperone 1 × 1 (O95456) Proteasome assembly chaperone 2 × 1 (Q969U7) Proteasome subunit beta type-7 × 1 (Q99436) Proteasome subunit beta type-3 × 1 (P49720) Proteasome subunit beta type-2 × 1 (P49721) Proteasome subunit beta type-5 × 1 (P28074) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.95 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 15
Chains and sequence ranges Author chain O; PDBConstruct 1–241; UniProt 1–241

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 8qz9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8qz9
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8qz9
Deposition date deposition_date2023-10-26
Structure title titleHuman 20S proteasome assembly intermediate structure 4
Keywords keywordsComplex, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.19
Radius of gyration Rg (electron density) rg_electron46.62
Forward intensity I(0) i01671640000.00
Molecular weight molecular_weight344450.0 kDa
Excluded volume excluded_volume432740 ų
Envelope volume envelope_volume613400 ų
Hydration-shell volume shell_volume104130 ų
Envelope diameter envelope_diameter152.3
Shell Rg shell_rg55.23
Envelope Rg envelope_rg45.87
Shape Rg shape_rg46.62
Total Rg total_rg46.95
Total atoms total_atoms24217
Residues n_residues3229
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 dmax148.6
Rg (real space) rg_real46.85
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real1.6720e+09
I(0) uncertainty (real space) i0_real_error2.9990e+07
Rg (reciprocal space) rg_reciprocal47.19
I(0) (reciprocal space) i0_reciprocal1672000000.0000
Solution quality estimate total_estimate0.8870
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary58.5
Skewness Skewness skewness0.110
Kurtosis Kurtosis kurtosis-0.488
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha249000000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.893; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.892

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

8. Citations (2)

9. Files and Curves (10)