6ef1

Yeast 26S proteasome bound to ubiquitinated substrate (5D motor state)

Method: ELECTRON MICROSCOPY Dmax: 143.5 Å Quality: GOOD

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

Proteasome subunit alpha type-1

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain A; UniProt 13–251 Not recorded Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Probable proteasome subunit alpha type-7 × 1 (P21242) 26S proteasome regulatory subunit 7 homolog × 1 (P33299) 26S proteasome regulatory subunit 4 homolog × 1 (P40327) 26S proteasome regulatory subunit 8 homolog × 1 (Q01939) 26S proteasome regulatory subunit 6B homolog × 1 (P33298) 26S proteasome subunit RPT4 × 1 (P53549) 26S proteasome regulatory subunit 6A × 1 (P33297) model substrate polypeptide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;specimens were manually blotted with Whatman #1 filter paper Resolution 4.73 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 1–239; UniProt 13–251

Proteasome subunit alpha type-2

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain B; UniProt 1–250 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-3 × 1 (P23638) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Probable proteasome subunit alpha type-7 × 1 (P21242) 26S proteasome regulatory subunit 7 homolog × 1 (P33299) 26S proteasome regulatory subunit 4 homolog × 1 (P40327) 26S proteasome regulatory subunit 8 homolog × 1 (Q01939) 26S proteasome regulatory subunit 6B homolog × 1 (P33298) 26S proteasome subunit RPT4 × 1 (P53549) 26S proteasome regulatory subunit 6A × 1 (P33297) model substrate polypeptide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;specimens were manually blotted with Whatman #1 filter paper Resolution 4.73 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

Proteasome subunit alpha type-3

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain C; UniProt 8–245 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Probable proteasome subunit alpha type-7 × 1 (P21242) 26S proteasome regulatory subunit 7 homolog × 1 (P33299) 26S proteasome regulatory subunit 4 homolog × 1 (P40327) 26S proteasome regulatory subunit 8 homolog × 1 (Q01939) 26S proteasome regulatory subunit 6B homolog × 1 (P33298) 26S proteasome subunit RPT4 × 1 (P53549) 26S proteasome regulatory subunit 6A × 1 (P33297) model substrate polypeptide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;specimens were manually blotted with Whatman #1 filter paper Resolution 4.73 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 1–238; UniProt 8–245

Proteasome subunit alpha type-4

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain D; UniProt 9–242 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Probable proteasome subunit alpha type-7 × 1 (P21242) 26S proteasome regulatory subunit 7 homolog × 1 (P33299) 26S proteasome regulatory subunit 4 homolog × 1 (P40327) 26S proteasome regulatory subunit 8 homolog × 1 (Q01939) 26S proteasome regulatory subunit 6B homolog × 1 (P33298) 26S proteasome subunit RPT4 × 1 (P53549) 26S proteasome regulatory subunit 6A × 1 (P33297) model substrate polypeptide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;specimens were manually blotted with Whatman #1 filter paper Resolution 4.73 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 1–234; UniProt 9–242

Proteasome subunit alpha type-5

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain E; UniProt 9–250 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-6 × 1 (P40302) Probable proteasome subunit alpha type-7 × 1 (P21242) 26S proteasome regulatory subunit 7 homolog × 1 (P33299) 26S proteasome regulatory subunit 4 homolog × 1 (P40327) 26S proteasome regulatory subunit 8 homolog × 1 (Q01939) 26S proteasome regulatory subunit 6B homolog × 1 (P33298) 26S proteasome subunit RPT4 × 1 (P53549) 26S proteasome regulatory subunit 6A × 1 (P33297) model substrate polypeptide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;specimens were manually blotted with Whatman #1 filter paper Resolution 4.73 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 1–242; UniProt 9–250

Proteasome subunit alpha type-6

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain F; UniProt 2–234 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Probable proteasome subunit alpha type-7 × 1 (P21242) 26S proteasome regulatory subunit 7 homolog × 1 (P33299) 26S proteasome regulatory subunit 4 homolog × 1 (P40327) 26S proteasome regulatory subunit 8 homolog × 1 (Q01939) 26S proteasome regulatory subunit 6B homolog × 1 (P33298) 26S proteasome subunit RPT4 × 1 (P53549) 26S proteasome regulatory subunit 6A × 1 (P33297) model substrate polypeptide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;specimens were manually blotted with Whatman #1 filter paper Resolution 4.73 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 1–233; UniProt 2–234

Probable proteasome subunit alpha type-7

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain G; UniProt 6–248 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) 26S proteasome regulatory subunit 7 homolog × 1 (P33299) 26S proteasome regulatory subunit 4 homolog × 1 (P40327) 26S proteasome regulatory subunit 8 homolog × 1 (Q01939) 26S proteasome regulatory subunit 6B homolog × 1 (P33298) 26S proteasome subunit RPT4 × 1 (P53549) 26S proteasome regulatory subunit 6A × 1 (P33297) model substrate polypeptide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;specimens were manually blotted with Whatman #1 filter paper Resolution 4.73 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 1–243; UniProt 6–248

26S proteasome regulatory subunit 7 homolog

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P33299

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain H; UniProt 194–455 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Probable proteasome subunit alpha type-7 × 1 (P21242) 26S proteasome regulatory subunit 4 homolog × 1 (P40327) 26S proteasome regulatory subunit 8 homolog × 1 (Q01939) 26S proteasome regulatory subunit 6B homolog × 1 (P33298) 26S proteasome subunit RPT4 × 1 (P53549) 26S proteasome regulatory subunit 6A × 1 (P33297) model substrate polypeptide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;specimens were manually blotted with Whatman #1 filter paper Resolution 4.73 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.

32 other PDB entries and 39 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRS7_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–262; UniProt 194–455

26S proteasome regulatory subunit 4 homolog

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P40327

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain I; UniProt 167–437 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Probable proteasome subunit alpha type-7 × 1 (P21242) 26S proteasome regulatory subunit 7 homolog × 1 (P33299) 26S proteasome regulatory subunit 8 homolog × 1 (Q01939) 26S proteasome regulatory subunit 6B homolog × 1 (P33298) 26S proteasome subunit RPT4 × 1 (P53549) 26S proteasome regulatory subunit 6A × 1 (P33297) model substrate polypeptide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;specimens were manually blotted with Whatman #1 filter paper Resolution 4.73 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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRS4_YEAST
Isoform
PDB entities 9
Chains and sequence ranges Author chain I; PDBConstruct 1–271; UniProt 167–437

26S proteasome regulatory subunit 8 homolog

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt Q01939

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain J; UniProt 133–405 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Probable proteasome subunit alpha type-7 × 1 (P21242) 26S proteasome regulatory subunit 7 homolog × 1 (P33299) 26S proteasome regulatory subunit 4 homolog × 1 (P40327) 26S proteasome regulatory subunit 6B homolog × 1 (P33298) 26S proteasome subunit RPT4 × 1 (P53549) 26S proteasome regulatory subunit 6A × 1 (P33297) model substrate polypeptide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;specimens were manually blotted with Whatman #1 filter paper Resolution 4.73 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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRS8_YEAST
Isoform
PDB entities 10
Chains and sequence ranges Author chain J; PDBConstruct 1–273; UniProt 133–405

26S proteasome regulatory subunit 6B homolog

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P33298

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain K; UniProt 153–428 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Probable proteasome subunit alpha type-7 × 1 (P21242) 26S proteasome regulatory subunit 7 homolog × 1 (P33299) 26S proteasome regulatory subunit 4 homolog × 1 (P40327) 26S proteasome regulatory subunit 8 homolog × 1 (Q01939) 26S proteasome subunit RPT4 × 1 (P53549) 26S proteasome regulatory subunit 6A × 1 (P33297) model substrate polypeptide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;specimens were manually blotted with Whatman #1 filter paper Resolution 4.73 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.

31 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRS6B_YEAST
Isoform
PDB entities 11
Chains and sequence ranges Author chain K; PDBConstruct 1–276; UniProt 153–428

26S proteasome subunit RPT4

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P53549

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain L; UniProt 166–436 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Probable proteasome subunit alpha type-7 × 1 (P21242) 26S proteasome regulatory subunit 7 homolog × 1 (P33299) 26S proteasome regulatory subunit 4 homolog × 1 (P40327) 26S proteasome regulatory subunit 8 homolog × 1 (Q01939) 26S proteasome regulatory subunit 6B homolog × 1 (P33298) 26S proteasome regulatory subunit 6A × 1 (P33297) model substrate polypeptide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;specimens were manually blotted with Whatman #1 filter paper Resolution 4.73 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.

29 other PDB entries and 29 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRS10_YEAST
Isoform
PDB entities 12
Chains and sequence ranges Author chain L; PDBConstruct 1–271; UniProt 166–436

26S proteasome regulatory subunit 6A

Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

UniProt P33297

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 × 14 PDB declaration: tetradecameric(14) Consistent with protein copy count Chain M; UniProt 173–434 Not recorded Proteasome subunit alpha type-1 × 1 (P21243) Proteasome subunit alpha type-2 × 1 (P23639) Proteasome subunit alpha type-3 × 1 (P23638) Proteasome subunit alpha type-4 × 1 (P40303) Proteasome subunit alpha type-5 × 1 (P32379) Proteasome subunit alpha type-6 × 1 (P40302) Probable proteasome subunit alpha type-7 × 1 (P21242) 26S proteasome regulatory subunit 7 homolog × 1 (P33299) 26S proteasome regulatory subunit 4 homolog × 1 (P40327) 26S proteasome regulatory subunit 8 homolog × 1 (Q01939) 26S proteasome regulatory subunit 6B homolog × 1 (P33298) 26S proteasome subunit RPT4 × 1 (P53549) model substrate polypeptide × 1 ATP ADENOSINE-5'-TRIPHOSPHATE × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE;specimens were manually blotted with Whatman #1 filter paper Resolution 4.73 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.

31 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRS6A_YEAST
Isoform
PDB entities 13
Chains and sequence ranges Author chain M; PDBConstruct 1–262; UniProt 173–434

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 6ef1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6ef1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6ef1
Deposition date deposition_date2018-08-15
Structure title titleYeast 26S proteasome bound to ubiquitinated substrate (5D motor state)
Keywords keywords26S Proteasome, ATPase, AAA+, Protease, Motor protein, Ubiquitin; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.46
Radius of gyration Rg (electron density) rg_electron46.58
Forward intensity I(0) i01671090000.00
Molecular weight molecular_weight335630.0 kDa
Excluded volume excluded_volume418250 ų
Envelope volume envelope_volume655080 ų
Hydration-shell volume shell_volume110990 ų
Envelope diameter envelope_diameter146.8
Shell Rg shell_rg56.53
Envelope Rg envelope_rg44.79
Shape Rg shape_rg46.58
Total Rg total_rg46.96
Total atoms total_atoms23658
Residues n_residues3294
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_real46.99
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real1.6710e+09
I(0) uncertainty (real space) i0_real_error3.4290e+07
Rg (reciprocal space) rg_reciprocal47.46
I(0) (reciprocal space) i0_reciprocal1672000000.0000
Solution quality estimate total_estimate0.8911
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary65.2
Skewness Skewness skewness-0.023
Kurtosis Kurtosis kurtosis-0.559
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha287800000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.901; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.940; Smooth: 0.937

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

8. Citations (1)

9. Files and Curves (10)