7teo

Cryo-EM structure of the 20S Alpha 3 Deletion proteasome core particle in complex with FUB1

Method: ELECTRON MICROSCOPY Dmax: 196.2 Å Quality: GOOD

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

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain 1; UniProt 1–241 Chain M; UniProt 1–241 Not recorded Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-4 × 4 (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-1 × 2 (P38624) 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) Silencing boundary-establishment protein FUB1 × 2 (P25659) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added to the sample immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 1
Chains and sequence ranges Author chain 1; PDBConstruct 1–241; UniProt 1–241 Author chain M; PDBConstruct 1–241; UniProt 1–241

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain 2; UniProt 1–266 Chain N; UniProt 1–266 Not recorded Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-4 × 4 (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-1 × 2 (P38624) 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) Silencing boundary-establishment protein FUB1 × 2 (P25659) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added to the sample immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 2
Chains and sequence ranges Author chain 2; PDBConstruct 1–266; UniProt 1–266 Author chain N; PDBConstruct 1–266; UniProt 1–266

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain A; UniProt 1–252 Chain O; UniProt 1–252 Not recorded Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-4 × 4 (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-1 × 2 (P38624) 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) Silencing boundary-establishment protein FUB1 × 2 (P25659) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added to the sample immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 3
Chains and sequence ranges Author chain A; PDBConstruct 1–252; UniProt 1–252 Author chain O; 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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain B; UniProt 1–250 Chain P; UniProt 1–250 Not recorded Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-4 × 4 (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-1 × 2 (P38624) 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) Silencing boundary-establishment protein FUB1 × 2 (P25659) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added to the sample immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 4
Chains and sequence ranges Author chain B; PDBConstruct 1–250; UniProt 1–250 Author chain P; PDBConstruct 1–250; UniProt 1–250

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain C; UniProt 1–254 Chain D; UniProt 1–254 Chain Q; UniProt 1–254 Chain R; UniProt 1–254 Not recorded Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) 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-1 × 2 (P38624) 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) Silencing boundary-establishment protein FUB1 × 2 (P25659) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added to the sample immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 5
Chains and sequence ranges Author chain C; PDBConstruct 1–254; UniProt 1–254 Author chain D; PDBConstruct 1–254; UniProt 1–254 Author chain Q; PDBConstruct 1–254; UniProt 1–254 Author chain R; 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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain E; UniProt 1–260 Chain S; UniProt 1–260 Not recorded Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-4 × 4 (P40303) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit beta type-1 × 2 (P38624) 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) Silencing boundary-establishment protein FUB1 × 2 (P25659) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added to the sample immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 6
Chains and sequence ranges Author chain E; PDBConstruct 1–260; UniProt 1–260 Author chain S; 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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain F; UniProt 1–234 Chain T; UniProt 1–234 Not recorded Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-4 × 4 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit beta type-1 × 2 (P38624) 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) Silencing boundary-establishment protein FUB1 × 2 (P25659) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added to the sample immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 7
Chains and sequence ranges Author chain F; PDBConstruct 1–234; UniProt 1–234 Author chain T; 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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain G; UniProt 1–288 Chain U; UniProt 1–288 Not recorded Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-4 × 4 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit beta type-1 × 2 (P38624) 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) Silencing boundary-establishment protein FUB1 × 2 (P25659) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added to the sample immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 8
Chains and sequence ranges Author chain G; PDBConstruct 1–288; UniProt 1–288 Author chain U; PDBConstruct 1–288; UniProt 1–288

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain H; UniProt 1–215 Chain V; UniProt 1–215 Not recorded Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-4 × 4 (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) Silencing boundary-establishment protein FUB1 × 2 (P25659) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added to the sample immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 9
Chains and sequence ranges Author chain H; PDBConstruct 1–215; UniProt 1–215 Author chain V; PDBConstruct 1–215; UniProt 1–215

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain I; UniProt 1–261 Chain W; UniProt 1–261 Not recorded Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-4 × 4 (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-1 × 2 (P38624) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Silencing boundary-establishment protein FUB1 × 2 (P25659) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added to the sample immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 10
Chains and sequence ranges Author chain I; PDBConstruct 1–261; UniProt 1–261 Author chain W; 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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain J; UniProt 1–205 Chain X; UniProt 1–205 Not recorded Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-4 × 4 (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-1 × 2 (P38624) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Silencing boundary-establishment protein FUB1 × 2 (P25659) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added to the sample immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 11
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-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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain K; UniProt 1–198 Chain Y; UniProt 1–198 Not recorded Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-4 × 4 (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-1 × 2 (P38624) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-5 × 2 (P30656) Silencing boundary-establishment protein FUB1 × 2 (P25659) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added to the sample immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 12
Chains and sequence ranges Author chain K; PDBConstruct 1–198; UniProt 1–198 Author chain Y; 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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain L; UniProt 1–287 Chain Z; UniProt 1–287 Not recorded Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-4 × 4 (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-1 × 2 (P38624) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Silencing boundary-establishment protein FUB1 × 2 (P25659) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added to the sample immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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 13
Chains and sequence ranges Author chain L; PDBConstruct 1–287; UniProt 1–287 Author chain Z; PDBConstruct 1–287; UniProt 1–287

Silencing boundary-establishment protein FUB1

OrganismNot specified

UniProt P25659

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 × 30 PDB declaration: 30-meric(30) Consistent with protein copy count Chain a; UniProt 1–250 Chain b; UniProt 1–250 Not recorded Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-4 × 4 (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-1 × 2 (P38624) 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) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Fluorinated Fos-Choline was added to the sample immediately prior to deposition on a grid for plunge freezing. cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.97 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name FUB1_YEAST
Isoform
PDB entities 14
Chains and sequence ranges Author chain a; PDBConstruct 1–250; UniProt 1–250 Author chain b; PDBConstruct 1–250; UniProt 1–250

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 7teo

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7teo
Deposition date deposition_date2022-01-05
Structure title titleCryo-EM structure of the 20S Alpha 3 Deletion proteasome core particle in complex with FUB1
Keywords keywordsPI31, core particle, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier59.39
Radius of gyration Rg (electron density) rg_electron58.95
Forward intensity I(0) i06663110000.00
Molecular weight molecular_weight694160.0 kDa
Excluded volume excluded_volume870570 ų
Envelope volume envelope_volume1229000 ų
Hydration-shell volume shell_volume165490 ų
Envelope diameter envelope_diameter192.2
Shell Rg shell_rg67.52
Envelope Rg envelope_rg57.61
Shape Rg shape_rg58.93
Total Rg total_rg59.20
Total atoms total_atoms97522
Residues n_residues6288
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 dmax196.2
Rg (real space) rg_real59.12
Rg uncertainty (real space) rg_real_error1.42
I(0) (real space) i0_real6.6630e+09
I(0) uncertainty (real space) i0_real_error1.3610e+08
Rg (reciprocal space) rg_reciprocal59.59
I(0) (reciprocal space) i0_reciprocal6668000000.0000
Solution quality estimate total_estimate0.8483
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary75.5
Skewness Skewness skewness0.239
Kurtosis Kurtosis kurtosis-0.337
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha1045000000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.750; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.947; Smooth: 0.827

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_id7teo101
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_id7teoB01
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_id7teoC01
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_id7teoD01
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_id7teoE01
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_id7teoG01
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_id7teoH01
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_id7teoI01
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_id7teoM01
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_id7teoP01
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_id7teoQ01
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_id7teoR01
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_id7teoS01
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_id7teoU01
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_id7teoV01
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_id7teoW01
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)