7v5m

20S+monoUb-CyclinB1-NT (S2)

Method: ELECTRON MICROSCOPY Dmax: 172.0 Å Quality: GOOD

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

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain A; UniProt 1–246 Chain O; 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-6 × 2 (P28072) 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 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.88 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–246; UniProt 1–246 Author chain O; PDBConstruct 1–246; UniProt 1–246

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain B; UniProt 1–234 Chain P; UniProt 1–234 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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-6 × 2 (P28072) 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 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.88 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–234; UniProt 1–234 Author chain P; 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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain C; UniProt 1–261 Chain Q; UniProt 1–261 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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 beta type-6 × 2 (P28072) 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 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.88 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–261; UniProt 1–261 Author chain Q; 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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain D; UniProt 1–248 Chain R; UniProt 1–248 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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 beta type-6 × 2 (P28072) 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 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.88 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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–248; UniProt 1–248 Author chain R; 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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain E; UniProt 1–241 Chain S; UniProt 1–241 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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 beta type-6 × 2 (P28072) 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 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.88 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 5
Chains and sequence ranges Author chain E; PDBConstruct 1–241; UniProt 1–241 Author chain S; 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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain F; UniProt 1–263 Chain T; UniProt 1–263 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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 beta type-6 × 2 (P28072) 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 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.88 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 6
Chains and sequence ranges Author chain F; PDBConstruct 1–263; UniProt 1–263 Author chain T; 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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain G; UniProt 1–255 Chain U; UniProt 1–255 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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 beta type-6 × 2 (P28072) 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 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.88 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 7
Chains and sequence ranges Author chain G; PDBConstruct 1–255; UniProt 1–255 Author chain U; PDBConstruct 1–255; UniProt 1–255

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain H; UniProt 35–239 Chain V; UniProt 35–239 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.88 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 8
Chains and sequence ranges Author chain H; PDBConstruct 1–205; UniProt 35–239 Author chain V; PDBConstruct 1–205; UniProt 35–239

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain I; UniProt 44–277 Chain W; UniProt 44–277 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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-6 × 2 (P28072) 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 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.88 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 9
Chains and sequence ranges Author chain I; PDBConstruct 1–234; UniProt 44–277 Author chain W; PDBConstruct 1–234; UniProt 44–277

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain J; UniProt 1–205 Chain X; UniProt 1–205 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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-6 × 2 (P28072) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.88 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 10
Chains and sequence ranges Author chain J; PDBConstruct 1–205; UniProt 1–205 Author chain X; 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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain K; UniProt 1–201 Chain Y; UniProt 1–201 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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-6 × 2 (P28072) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.88 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 11
Chains and sequence ranges Author chain K; PDBConstruct 1–201; UniProt 1–201 Author chain Y; 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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain L; UniProt 60–263 Chain Z; UniProt 60–263 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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-6 × 2 (P28072) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.88 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 12
Chains and sequence ranges Author chain L; PDBConstruct 1–204; UniProt 60–263 Author chain Z; PDBConstruct 1–204; UniProt 60–263

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain M; UniProt 29–241 Chain a; UniProt 29–241 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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-6 × 2 (P28072) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.88 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 13
Chains and sequence ranges Author chain M; PDBConstruct 1–213; UniProt 29–241 Author chain a; PDBConstruct 1–213; UniProt 29–241

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain N; UniProt 46–264 Chain b; UniProt 46–264 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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-6 × 2 (P28072) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.88 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 14
Chains and sequence ranges Author chain N; PDBConstruct 1–219; UniProt 46–264 Author chain b; PDBConstruct 1–219; UniProt 46–264

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 7v5m

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7v5m
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7v5m
Deposition date deposition_date2021-08-17
Structure title title20S+monoUb-CyclinB1-NT (S2)
Keywords keywords20S proteasome, human, substrate, ubiquitin, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier59.34
Radius of gyration Rg (electron density) rg_electron58.96
Forward intensity I(0) i05636530000.00
Molecular weight molecular_weight644190.0 kDa
Excluded volume excluded_volume810800 ų
Envelope volume envelope_volume1189900 ų
Hydration-shell volume shell_volume162450 ų
Envelope diameter envelope_diameter194.5
Shell Rg shell_rg66.63
Envelope Rg envelope_rg56.87
Shape Rg shape_rg58.98
Total Rg total_rg59.05
Total atoms total_atoms45340
Residues n_residues6198
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 dmax172.0
Rg (real space) rg_real59.09
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real5.6360e+09
I(0) uncertainty (real space) i0_real_error1.0620e+08
Rg (reciprocal space) rg_reciprocal59.53
I(0) (reciprocal space) i0_reciprocal5640000000.0000
Solution quality estimate total_estimate0.8319
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary72.8
Skewness Skewness skewness0.223
Kurtosis Kurtosis kurtosis-0.410
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha680100000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.941; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.986; Smooth: 0.004

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

7. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

Domain ID domain_id7v5mB01
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_id7v5mC01
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_id7v5mD01
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_id7v5mE01
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_id7v5mI01
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_id7v5mL01
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_id7v5mM01
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_id7v5mN01
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_id7v5mP01
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_id7v5mQ01
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_id7v5mR01
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_id7v5mS01
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_id7v5mW01
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_id7v5mZ01
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_id7v5ma01
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_id7v5mb01
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

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9. Files and Curves (10)