8u6y

Preholo-Proteasome from Beta 3 D205 deletion

Method: ELECTRON MICROSCOPY Dmax: 249.2 Å Quality: GOOD

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

Proteasome subunit alpha type-1

OrganismNot specified

UniProt P21243

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 1–252 Chain R; UniProt 1–252 Not recorded Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) Proteasome chaperone 1 × 2 (Q05778) Proteasome assembly chaperone 2 × 2 (P36040) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

374 other PDB entries and 375 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA1_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–252; UniProt 1–252 Author chain R; PDBConstruct 1–252; UniProt 1–252

Proteasome subunit alpha type-2

OrganismNot specified

UniProt P23639

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 1–250 Chain S; UniProt 1–250 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) Proteasome chaperone 1 × 2 (Q05778) Proteasome assembly chaperone 2 × 2 (P36040) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

373 other PDB entries and 374 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA2_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–250; UniProt 1–250 Author chain S; PDBConstruct 1–250; UniProt 1–250

Proteasome subunit alpha type-3

OrganismNot specified

UniProt P23638

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 1–245 Chain T; UniProt 1–245 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) Proteasome chaperone 1 × 2 (Q05778) Proteasome assembly chaperone 2 × 2 (P36040) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

371 other PDB entries and 372 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA3_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–245; UniProt 1–245 Author chain T; PDBConstruct 1–245; UniProt 1–245

Proteasome subunit alpha type-4

OrganismNot specified

UniProt P40303

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 1–254 Chain U; UniProt 1–254 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) Proteasome chaperone 1 × 2 (Q05778) Proteasome assembly chaperone 2 × 2 (P36040) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

373 other PDB entries and 374 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA4_YEAST
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–254; UniProt 1–254 Author chain U; PDBConstruct 1–254; UniProt 1–254

Proteasome subunit alpha type-5

OrganismNot specified

UniProt P32379

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 1–260 Chain V; UniProt 1–260 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) Proteasome chaperone 1 × 2 (Q05778) Proteasome assembly chaperone 2 × 2 (P36040) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

373 other PDB entries and 375 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA5_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–260; UniProt 1–260 Author chain V; PDBConstruct 1–260; UniProt 1–260

Proteasome subunit alpha type-6

OrganismNot specified

UniProt P40302

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 1–234 Chain W; UniProt 1–234 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) Proteasome chaperone 1 × 2 (Q05778) Proteasome assembly chaperone 2 × 2 (P36040) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

371 other PDB entries and 372 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA6_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–234; UniProt 1–234 Author chain W; PDBConstruct 1–234; UniProt 1–234

Proteasome subunit alpha type-7

OrganismNot specified

UniProt P21242

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 1–288 Chain X; UniProt 1–288 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) Proteasome chaperone 1 × 2 (Q05778) Proteasome assembly chaperone 2 × 2 (P36040) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

372 other PDB entries and 373 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA7_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–288; UniProt 1–288 Author chain X; PDBConstruct 1–288; UniProt 1–288

Proteasome maturation factor UMP1

OrganismNot specified

UniProt P38293

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 1–148 Chain Y; UniProt 1–148 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) Proteasome chaperone 1 × 2 (Q05778) Proteasome assembly chaperone 2 × 2 (P36040) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UMP1_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–148; UniProt 1–148 Author chain Y; PDBConstruct 1–148; UniProt 1–148

Proteasome subunit beta type-2

OrganismNot specified

UniProt P25043

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 1–261 Chain Z; UniProt 1–261 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) Proteasome chaperone 1 × 2 (Q05778) Proteasome assembly chaperone 2 × 2 (P36040) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

358 other PDB entries and 359 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB2_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain I; PDBConstruct 1–261; UniProt 1–261 Author chain Z; PDBConstruct 1–261; UniProt 1–261

Proteasome subunit beta type-3

OrganismNot specified

UniProt P25451

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 1–204 Chain a; UniProt 1–204 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) Proteasome chaperone 1 × 2 (Q05778) Proteasome assembly chaperone 2 × 2 (P36040) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

369 other PDB entries and 370 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB3_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain J; PDBConstruct 1–204; UniProt 1–204 Author chain a; PDBConstruct 1–204; UniProt 1–204

Proteasome subunit beta type-4

OrganismNot specified

UniProt P22141

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 1–198 Chain b; UniProt 1–198 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) Proteasome chaperone 1 × 2 (Q05778) Proteasome assembly chaperone 2 × 2 (P36040) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

369 other PDB entries and 370 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB4_YEAST
Isoform
PDB entities 11
Chains and sequence ranges Author chain K; PDBConstruct 1–198; UniProt 1–198 Author chain b; PDBConstruct 1–198; UniProt 1–198

Proteasome subunit beta type-5

OrganismNot specified

UniProt P30656

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 1–287 Chain c; UniProt 1–287 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) Proteasome chaperone 1 × 2 (Q05778) Proteasome assembly chaperone 2 × 2 (P36040) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

360 other PDB entries and 361 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB5_YEAST
Isoform
PDB entities 12
Chains and sequence ranges Author chain L; PDBConstruct 1–287; UniProt 1–287 Author chain c; PDBConstruct 1–287; UniProt 1–287

Proteasome subunit beta type-6

OrganismNot specified

UniProt P23724

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 1–241 Chain d; UniProt 1–241 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-1 × 2 (P38624) Proteasome chaperone 1 × 2 (Q05778) Proteasome assembly chaperone 2 × 2 (P36040) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

359 other PDB entries and 360 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB6_YEAST
Isoform
PDB entities 13
Chains and sequence ranges Author chain M; PDBConstruct 1–241; UniProt 1–241 Author chain d; PDBConstruct 1–241; UniProt 1–241

Proteasome subunit beta type-1

OrganismNot specified

UniProt P38624

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 1–215 Chain e; UniProt 1–215 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome chaperone 1 × 2 (Q05778) Proteasome assembly chaperone 2 × 2 (P36040) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

365 other PDB entries and 366 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB1_YEAST
Isoform
PDB entities 14
Chains and sequence ranges Author chain N; PDBConstruct 1–215; UniProt 1–215 Author chain e; PDBConstruct 1–215; UniProt 1–215

Proteasome chaperone 1

OrganismNot specified

UniProt Q05778

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 1–276 Chain f; UniProt 1–276 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) Proteasome assembly chaperone 2 × 2 (P36040) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POC1_YEAST
Isoform
PDB entities 15
Chains and sequence ranges Author chain O; PDBConstruct 1–276; UniProt 1–276 Author chain f; PDBConstruct 1–276; UniProt 1–276

Proteasome assembly chaperone 2

OrganismNot specified

UniProt P36040

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 1–267 Chain g; UniProt 1–267 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) Proteasome chaperone 1 × 2 (Q05778) Proteasome subunit beta type-7 × 2 (P30657) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name POC2_YEAST
Isoform
PDB entities 16
Chains and sequence ranges Author chain P; PDBConstruct 1–267; UniProt 1–267 Author chain g; PDBConstruct 1–267; UniProt 1–267

Proteasome subunit beta type-7

OrganismNot specified

UniProt P30657

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 1–266 Chain h; UniProt 1–266 Not recorded Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome maturation factor UMP1 × 2 (P38293) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) Proteasome chaperone 1 × 2 (Q05778) Proteasome assembly chaperone 2 × 2 (P36040) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.80 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.

358 other PDB entries and 359 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB7_YEAST
Isoform
PDB entities 17
Chains and sequence ranges Author chain Q; PDBConstruct 1–266; UniProt 1–266 Author chain h; PDBConstruct 1–266; UniProt 1–266

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 8u6y

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8u6y
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8u6y
Deposition date deposition_date2023-09-14
Structure title titlePreholo-Proteasome from Beta 3 D205 deletion
Keywords keywordsProteasome, core particle, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier65.69
Radius of gyration Rg (electron density) rg_electron66.20
Forward intensity I(0) i08836510000.00
Molecular weight molecular_weight810080.0 kDa
Excluded volume excluded_volume1019100 ų
Envelope volume envelope_volume1419500 ų
Hydration-shell volume shell_volume175870 ų
Envelope diameter envelope_diameter241.2
Shell Rg shell_rg70.61
Envelope Rg envelope_rg64.61
Shape Rg shape_rg66.19
Total Rg total_rg66.31
Total atoms total_atoms113955
Residues n_residues7304
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 dmax249.2
Rg (real space) rg_real69.80
Rg uncertainty (real space) rg_real_error1.56
I(0) (real space) i0_real8.9160e+09
I(0) uncertainty (real space) i0_real_error1.9300e+08
Rg (reciprocal space) rg_reciprocal65.50
I(0) (reciprocal space) i0_reciprocal8830000000.0000
Solution quality estimate total_estimate0.8554
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary72.7
Skewness Skewness skewness0.673
Kurtosis Kurtosis kurtosis0.215
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.9380
Highest regularization parameter α highest_alpha1476000000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.612; Stabil: 0.853; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.763

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (17)

8. Citations (1)

9. Files and Curves (10)