8qys

Human preholo proteasome 20S core particle

Method: ELECTRON MICROSCOPY Dmax: 258.1 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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain A; UniProt 1–234 Chain R; 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 maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 1 × 2 (O95456) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 R; 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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain B; UniProt 3–250 Chain S; UniProt 3–250 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 maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 1 × 2 (O95456) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 1–248; UniProt 3–250 Author chain S; PDBConstruct 1–248; UniProt 3–250

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain C; UniProt 3–236 Chain T; UniProt 3–236 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 maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 1 × 2 (O95456) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 1–234; UniProt 3–236 Author chain T; PDBConstruct 1–234; UniProt 3–236

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain D; UniProt 1–240 Chain U; UniProt 1–240 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 maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 1 × 2 (O95456) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 1–240; UniProt 1–240 Author chain U; PDBConstruct 1–240; UniProt 1–240

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain E; UniProt 1–241 Chain V; 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-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 1 × 2 (O95456) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 1–241; UniProt 1–241 Author chain V; PDBConstruct 1–241; UniProt 1–241

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain F; UniProt 5–245 Chain W; UniProt 5–245 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 maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 1 × 2 (O95456) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 1–241; UniProt 5–245 Author chain W; PDBConstruct 1–241; UniProt 5–245

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain G; UniProt 1–244 Chain X; UniProt 1–244 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 maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 1 × 2 (O95456) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 1–244; UniProt 1–244 Author chain X; PDBConstruct 1–244; UniProt 1–244

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain H; UniProt 1–141 Chain Y; UniProt 1–141 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 assembly chaperone 1 × 2 (O95456) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 Author chain Y; 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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain I; UniProt 1–288 Chain Z; UniProt 1–288 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 maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 Author chain Z; 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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain J; 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 maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 1 × 2 (O95456) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 1–264; UniProt 1–264 Author chain a; PDBConstruct 1–264; 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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain K; UniProt 2–263 Chain b; UniProt 2–263 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 maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 1 × 2 (O95456) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 1–262; UniProt 2–263 Author chain b; PDBConstruct 1–262; UniProt 2–263

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain L; UniProt 3–205 Chain c; UniProt 3–205 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 maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 1 × 2 (O95456) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 1–203; UniProt 3–205 Author chain c; PDBConstruct 1–203; UniProt 3–205

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain M; UniProt 1–197 Chain d; UniProt 1–197 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 maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 1 × 2 (O95456) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 1–197; UniProt 1–197 Author chain d; PDBConstruct 1–197; UniProt 1–197

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain N; UniProt 52–259 Chain e; UniProt 52–259 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 maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 1 × 2 (O95456) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 1–208; UniProt 52–259 Author chain e; PDBConstruct 1–208; UniProt 52–259

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain O; UniProt 30–241 Chain f; UniProt 30–241 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 maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 1 × 2 (O95456) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 1–212; UniProt 30–241 Author chain f; PDBConstruct 1–212; UniProt 30–241

Proteasome subunit beta type-4

Homo sapiens

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain P; UniProt 50–257 Chain g; UniProt 50–257 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 maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 1 × 2 (O95456) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 16
Chains and sequence ranges Author chain P; PDBConstruct 1–208; UniProt 50–257 Author chain g; PDBConstruct 1–208; UniProt 50–257

Proteasome subunit beta type-6

Homo sapiens

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 × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain Q; UniProt 35–231 Chain h; UniProt 35–231 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 maturation protein × 2 (Q9Y244) Proteasome assembly chaperone 1 × 2 (O95456) Proteasome assembly chaperone 2 × 2 (Q969U7) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.89 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 17
Chains and sequence ranges Author chain Q; PDBConstruct 1–197; UniProt 35–231 Author chain h; PDBConstruct 1–197; UniProt 35–231

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 8qys

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8qys
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8qys
Deposition date deposition_date2023-10-26
Structure title titleHuman preholo proteasome 20S core particle
Keywords keywordsComplex, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier67.23
Radius of gyration Rg (electron density) rg_electron67.50
Forward intensity I(0) i09323320000.00
Molecular weight molecular_weight823660.0 kDa
Excluded volume excluded_volume1033000 ų
Envelope volume envelope_volume1543500 ų
Hydration-shell volume shell_volume187800 ų
Envelope diameter envelope_diameter249.0
Shell Rg shell_rg71.55
Envelope Rg envelope_rg66.20
Shape Rg shape_rg67.49
Total Rg total_rg67.56
Total atoms total_atoms57862
Residues n_residues7588
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 dmax258.1
Rg (real space) rg_real71.44
Rg uncertainty (real space) rg_real_error1.67
I(0) (real space) i0_real9.4170e+09
I(0) uncertainty (real space) i0_real_error2.0550e+08
Rg (reciprocal space) rg_reciprocal66.88
I(0) (reciprocal space) i0_reciprocal9316000000.0000
Solution quality estimate total_estimate0.8384
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary78.5
Skewness Skewness skewness0.721
Kurtosis Kurtosis kurtosis0.364
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.8664
Highest regularization parameter α highest_alpha1401000000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.538; Stabil: 0.855; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.767

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (17)

8. Citations (2)

9. Files and Curves (10)