9rm1

13S+Beta1+Beta5 proteasome precursor complex

Method: ELECTRON MICROSCOPY Dmax: 143.5 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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain A; UniProt 1–252 Not recorded Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Proteasome subunit beta type-1 × 1 (P38624) Proteasome maturation factor UMP1 × 1 (P38293) Proteasome chaperone 1 × 1 (Q05778) Proteasome assembly chaperone 2 × 1 (P36040) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Probable proteasome subunit alpha type-7 × 1 (P21242) Proteasome subunit beta type-2 × 1 (P25043) Proteasome subunit beta type-3 × 1 (P25451) Proteasome subunit beta type-4 × 1 (P22141) Proteasome subunit beta type-5 × 1 (P30656) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl 50 mM Tris-HCl cryo-EM vitrification conditions:Cryogen ETHANE;manual plunge freezing device purchased from "Neptune FLuid Flow Systems" Resolution 4.11 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

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain D; UniProt 1–254 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Proteasome subunit beta type-1 × 1 (P38624) Proteasome maturation factor UMP1 × 1 (P38293) Proteasome chaperone 1 × 1 (Q05778) Proteasome assembly chaperone 2 × 1 (P36040) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Probable proteasome subunit alpha type-7 × 1 (P21242) Proteasome subunit beta type-2 × 1 (P25043) Proteasome subunit beta type-3 × 1 (P25451) Proteasome subunit beta type-4 × 1 (P22141) Proteasome subunit beta type-5 × 1 (P30656) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl 50 mM Tris-HCl cryo-EM vitrification conditions:Cryogen ETHANE;manual plunge freezing device purchased from "Neptune FLuid Flow Systems" Resolution 4.11 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 2
Chains and sequence ranges Author chain D; 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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain E; UniProt 1–260 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-6 × 1 (P40302) Proteasome subunit beta type-1 × 1 (P38624) Proteasome maturation factor UMP1 × 1 (P38293) Proteasome chaperone 1 × 1 (Q05778) Proteasome assembly chaperone 2 × 1 (P36040) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Probable proteasome subunit alpha type-7 × 1 (P21242) Proteasome subunit beta type-2 × 1 (P25043) Proteasome subunit beta type-3 × 1 (P25451) Proteasome subunit beta type-4 × 1 (P22141) Proteasome subunit beta type-5 × 1 (P30656) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl 50 mM Tris-HCl cryo-EM vitrification conditions:Cryogen ETHANE;manual plunge freezing device purchased from "Neptune FLuid Flow Systems" Resolution 4.11 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 3
Chains and sequence ranges Author chain E; 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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain F; UniProt 1–234 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit beta type-1 × 1 (P38624) Proteasome maturation factor UMP1 × 1 (P38293) Proteasome chaperone 1 × 1 (Q05778) Proteasome assembly chaperone 2 × 1 (P36040) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Probable proteasome subunit alpha type-7 × 1 (P21242) Proteasome subunit beta type-2 × 1 (P25043) Proteasome subunit beta type-3 × 1 (P25451) Proteasome subunit beta type-4 × 1 (P22141) Proteasome subunit beta type-5 × 1 (P30656) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl 50 mM Tris-HCl cryo-EM vitrification conditions:Cryogen ETHANE;manual plunge freezing device purchased from "Neptune FLuid Flow Systems" Resolution 4.11 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 4
Chains and sequence ranges Author chain F; PDBConstruct 1–234; UniProt 1–234

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain H; UniProt 1–215 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Proteasome maturation factor UMP1 × 1 (P38293) Proteasome chaperone 1 × 1 (Q05778) Proteasome assembly chaperone 2 × 1 (P36040) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Probable proteasome subunit alpha type-7 × 1 (P21242) Proteasome subunit beta type-2 × 1 (P25043) Proteasome subunit beta type-3 × 1 (P25451) Proteasome subunit beta type-4 × 1 (P22141) Proteasome subunit beta type-5 × 1 (P30656) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl 50 mM Tris-HCl cryo-EM vitrification conditions:Cryogen ETHANE;manual plunge freezing device purchased from "Neptune FLuid Flow Systems" Resolution 4.11 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 5
Chains and sequence ranges Author chain H; PDBConstruct 1–215; UniProt 1–215

Proteasome maturation factor UMP1

Saccharomyces cerevisiae

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain 3; UniProt 1–148 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Proteasome subunit beta type-1 × 1 (P38624) Proteasome chaperone 1 × 1 (Q05778) Proteasome assembly chaperone 2 × 1 (P36040) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Probable proteasome subunit alpha type-7 × 1 (P21242) Proteasome subunit beta type-2 × 1 (P25043) Proteasome subunit beta type-3 × 1 (P25451) Proteasome subunit beta type-4 × 1 (P22141) Proteasome subunit beta type-5 × 1 (P30656) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl 50 mM Tris-HCl cryo-EM vitrification conditions:Cryogen ETHANE;manual plunge freezing device purchased from "Neptune FLuid Flow Systems" Resolution 4.11 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 6
Chains and sequence ranges Author chain 3; PDBConstruct 15–162; UniProt 1–148

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain 4; UniProt 1–276 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Proteasome subunit beta type-1 × 1 (P38624) Proteasome maturation factor UMP1 × 1 (P38293) Proteasome assembly chaperone 2 × 1 (P36040) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Probable proteasome subunit alpha type-7 × 1 (P21242) Proteasome subunit beta type-2 × 1 (P25043) Proteasome subunit beta type-3 × 1 (P25451) Proteasome subunit beta type-4 × 1 (P22141) Proteasome subunit beta type-5 × 1 (P30656) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl 50 mM Tris-HCl cryo-EM vitrification conditions:Cryogen ETHANE;manual plunge freezing device purchased from "Neptune FLuid Flow Systems" Resolution 4.11 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 7
Chains and sequence ranges Author chain 4; 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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain 5; UniProt 1–267 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Proteasome subunit beta type-1 × 1 (P38624) Proteasome maturation factor UMP1 × 1 (P38293) Proteasome chaperone 1 × 1 (Q05778) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Probable proteasome subunit alpha type-7 × 1 (P21242) Proteasome subunit beta type-2 × 1 (P25043) Proteasome subunit beta type-3 × 1 (P25451) Proteasome subunit beta type-4 × 1 (P22141) Proteasome subunit beta type-5 × 1 (P30656) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl 50 mM Tris-HCl cryo-EM vitrification conditions:Cryogen ETHANE;manual plunge freezing device purchased from "Neptune FLuid Flow Systems" Resolution 4.11 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 8
Chains and sequence ranges Author chain 5; PDBConstruct 1–267; UniProt 1–267

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain B; UniProt 1–250 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Proteasome subunit beta type-1 × 1 (P38624) Proteasome maturation factor UMP1 × 1 (P38293) Proteasome chaperone 1 × 1 (Q05778) Proteasome assembly chaperone 2 × 1 (P36040) Proteasome subunit alpha type-3 × 1 (P23638) Probable proteasome subunit alpha type-7 × 1 (P21242) Proteasome subunit beta type-2 × 1 (P25043) Proteasome subunit beta type-3 × 1 (P25451) Proteasome subunit beta type-4 × 1 (P22141) Proteasome subunit beta type-5 × 1 (P30656) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl 50 mM Tris-HCl cryo-EM vitrification conditions:Cryogen ETHANE;manual plunge freezing device purchased from "Neptune FLuid Flow Systems" Resolution 4.11 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 9
Chains and sequence ranges Author chain B; 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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain C; UniProt 1–258 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Proteasome subunit beta type-1 × 1 (P38624) Proteasome maturation factor UMP1 × 1 (P38293) Proteasome chaperone 1 × 1 (Q05778) Proteasome assembly chaperone 2 × 1 (P36040) Proteasome subunit alpha type-2 × 1 (P23639) Probable proteasome subunit alpha type-7 × 1 (P21242) Proteasome subunit beta type-2 × 1 (P25043) Proteasome subunit beta type-3 × 1 (P25451) Proteasome subunit beta type-4 × 1 (P22141) Proteasome subunit beta type-5 × 1 (P30656) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl 50 mM Tris-HCl cryo-EM vitrification conditions:Cryogen ETHANE;manual plunge freezing device purchased from "Neptune FLuid Flow Systems" Resolution 4.11 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 10
Chains and sequence ranges Author chain C; PDBConstruct 1–258; UniProt 1–258

Probable 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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain G; UniProt 1–288 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Proteasome subunit beta type-1 × 1 (P38624) Proteasome maturation factor UMP1 × 1 (P38293) Proteasome chaperone 1 × 1 (Q05778) Proteasome assembly chaperone 2 × 1 (P36040) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Proteasome subunit beta type-2 × 1 (P25043) Proteasome subunit beta type-3 × 1 (P25451) Proteasome subunit beta type-4 × 1 (P22141) Proteasome subunit beta type-5 × 1 (P30656) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl 50 mM Tris-HCl cryo-EM vitrification conditions:Cryogen ETHANE;manual plunge freezing device purchased from "Neptune FLuid Flow Systems" Resolution 4.11 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 11
Chains and sequence ranges Author chain G; PDBConstruct 1–288; UniProt 1–288

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain I; UniProt 1–261 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Proteasome subunit beta type-1 × 1 (P38624) Proteasome maturation factor UMP1 × 1 (P38293) Proteasome chaperone 1 × 1 (Q05778) Proteasome assembly chaperone 2 × 1 (P36040) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Probable proteasome subunit alpha type-7 × 1 (P21242) Proteasome subunit beta type-3 × 1 (P25451) Proteasome subunit beta type-4 × 1 (P22141) Proteasome subunit beta type-5 × 1 (P30656) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl 50 mM Tris-HCl cryo-EM vitrification conditions:Cryogen ETHANE;manual plunge freezing device purchased from "Neptune FLuid Flow Systems" Resolution 4.11 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 12
Chains and sequence ranges Author chain I; 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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain J; UniProt 1–205 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Proteasome subunit beta type-1 × 1 (P38624) Proteasome maturation factor UMP1 × 1 (P38293) Proteasome chaperone 1 × 1 (Q05778) Proteasome assembly chaperone 2 × 1 (P36040) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Probable proteasome subunit alpha type-7 × 1 (P21242) Proteasome subunit beta type-2 × 1 (P25043) Proteasome subunit beta type-4 × 1 (P22141) Proteasome subunit beta type-5 × 1 (P30656) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl 50 mM Tris-HCl cryo-EM vitrification conditions:Cryogen ETHANE;manual plunge freezing device purchased from "Neptune FLuid Flow Systems" Resolution 4.11 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 13
Chains and sequence ranges Author chain J; PDBConstruct 1–205; UniProt 1–205

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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain K; UniProt 1–198 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Proteasome subunit beta type-1 × 1 (P38624) Proteasome maturation factor UMP1 × 1 (P38293) Proteasome chaperone 1 × 1 (Q05778) Proteasome assembly chaperone 2 × 1 (P36040) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Probable proteasome subunit alpha type-7 × 1 (P21242) Proteasome subunit beta type-2 × 1 (P25043) Proteasome subunit beta type-3 × 1 (P25451) Proteasome subunit beta type-5 × 1 (P30656) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl 50 mM Tris-HCl cryo-EM vitrification conditions:Cryogen ETHANE;manual plunge freezing device purchased from "Neptune FLuid Flow Systems" Resolution 4.11 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 14
Chains and sequence ranges Author chain K; 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 × 15 PDB declaration: 15-meric(15) Consistent with protein copy count Chain L; UniProt 1–287 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Proteasome subunit beta type-1 × 1 (P38624) Proteasome maturation factor UMP1 × 1 (P38293) Proteasome chaperone 1 × 1 (Q05778) Proteasome assembly chaperone 2 × 1 (P36040) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Probable proteasome subunit alpha type-7 × 1 (P21242) Proteasome subunit beta type-2 × 1 (P25043) Proteasome subunit beta type-3 × 1 (P25451) Proteasome subunit beta type-4 × 1 (P22141) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;150 mM NaCl 50 mM Tris-HCl cryo-EM vitrification conditions:Cryogen ETHANE;manual plunge freezing device purchased from "Neptune FLuid Flow Systems" Resolution 4.11 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 15
Chains and sequence ranges Author chain L; PDBConstruct 1–287; UniProt 1–287

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 9rm1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9rm1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9rm1
Deposition date deposition_date2025-06-17
Structure title title13S+Beta1+Beta5 proteasome precursor complex
Keywords keywordsproteasome biogenesis, Ump1, Pba1-2, cryo-EM, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.79
Radius of gyration Rg (electron density) rg_electron46.25
Forward intensity I(0) i01318570000.00
Molecular weight molecular_weight185360.0 kDa
Excluded volume excluded_volume182470 ų
Envelope volume envelope_volume501500 ų
Hydration-shell volume shell_volume89493 ų
Envelope diameter envelope_diameter142.7
Shell Rg shell_rg52.39
Envelope Rg envelope_rg43.96
Shape Rg shape_rg46.25
Total Rg total_rg46.48
Total atoms total_atoms13220
Residues n_residues3305
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 dmax143.5
Rg (real space) rg_real46.45
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real1.3190e+09
I(0) uncertainty (real space) i0_real_error2.0880e+07
Rg (reciprocal space) rg_reciprocal46.79
I(0) (reciprocal space) i0_reciprocal1319000000.0000
Solution quality estimate total_estimate0.8874
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary59.1
Skewness Skewness skewness0.085
Kurtosis Kurtosis kurtosis-0.507
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha159700000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.923; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.957; Smooth: 0.806

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

8. Citations (1)

9. Files and Curves (10)