7o2l

Yeast 20S proteasome in complex with the covalently bound inhibitor b-lactone (2R,3S)-3-isopropyl-4-oxo-2-oxetane-carboxylate (IOC)

Method: X-RAY DIFFRACTION Dmax: 194.9 Å Quality: GOOD

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

HLJ1_G0039880.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A6L1BIF8

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain A; UniProt 1–250 Chain O; UniProt 1–250 Not recorded BJ4_G0021480.mRNA.1.CDS.1 × 2 (A0A6A5PXC6) HLJ1_G0048980.mRNA.1.CDS.1 × 2 (A0A6A5Q273) 20S proteasome × 2 (P32379) BJ4_G0043800.mRNA.1.CDS.1 × 2 (A0A6A5PTH4) Probable proteasome subunit alpha type-7 × 2 (A0A6A5Q4M4) BJ4_G0020160.mRNA.1.CDS.1 × 2 (A0A6A5PYC9) Proteasome endopeptidase complex × 2 (A0A6A5Q449) Proteasome endopeptidase complex × 2 (A0A6L0YA22) Proteasome subunit beta × 2 (A0A6A5Q0W2) Proteasome subunit beta type-5 × 2 (A0A6V8RU78) Proteasome endopeptidase complex × 2 (A0A6A5Q0P3) Proteasome subunit beta type-7 × 2 (P30657) Proteasome endopeptidase complex × 2 (A0A6L0ZSP2) MG MAGNESIUM ION × 8 CL CHLORIDE ION × 2 V08 (2 {R},3 {S})-3-methanoyl-4-methyl-2-hydroxy-pentanoic acid × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 3.00 Å R-free 0.216

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6L1BIF8_YEASX
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–250; UniProt 1–250 Author chain O; PDBConstruct 1–250; UniProt 1–250

BJ4_G0021480.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A6A5PXC6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain B; UniProt 1–258 Chain P; UniProt 1–258 Not recorded HLJ1_G0039880.mRNA.1.CDS.1 × 2 (A0A6L1BIF8) HLJ1_G0048980.mRNA.1.CDS.1 × 2 (A0A6A5Q273) 20S proteasome × 2 (P32379) BJ4_G0043800.mRNA.1.CDS.1 × 2 (A0A6A5PTH4) Probable proteasome subunit alpha type-7 × 2 (A0A6A5Q4M4) BJ4_G0020160.mRNA.1.CDS.1 × 2 (A0A6A5PYC9) Proteasome endopeptidase complex × 2 (A0A6A5Q449) Proteasome endopeptidase complex × 2 (A0A6L0YA22) Proteasome subunit beta × 2 (A0A6A5Q0W2) Proteasome subunit beta type-5 × 2 (A0A6V8RU78) Proteasome endopeptidase complex × 2 (A0A6A5Q0P3) Proteasome subunit beta type-7 × 2 (P30657) Proteasome endopeptidase complex × 2 (A0A6L0ZSP2) MG MAGNESIUM ION × 8 CL CHLORIDE ION × 2 V08 (2 {R},3 {S})-3-methanoyl-4-methyl-2-hydroxy-pentanoic acid × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 3.00 Å R-free 0.216

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5PXC6_YEASX
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–258; UniProt 1–258 Author chain P; PDBConstruct 1–258; UniProt 1–258

HLJ1_G0048980.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A6A5Q273

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain C; UniProt 1–254 Chain Q; UniProt 1–254 Not recorded HLJ1_G0039880.mRNA.1.CDS.1 × 2 (A0A6L1BIF8) BJ4_G0021480.mRNA.1.CDS.1 × 2 (A0A6A5PXC6) 20S proteasome × 2 (P32379) BJ4_G0043800.mRNA.1.CDS.1 × 2 (A0A6A5PTH4) Probable proteasome subunit alpha type-7 × 2 (A0A6A5Q4M4) BJ4_G0020160.mRNA.1.CDS.1 × 2 (A0A6A5PYC9) Proteasome endopeptidase complex × 2 (A0A6A5Q449) Proteasome endopeptidase complex × 2 (A0A6L0YA22) Proteasome subunit beta × 2 (A0A6A5Q0W2) Proteasome subunit beta type-5 × 2 (A0A6V8RU78) Proteasome endopeptidase complex × 2 (A0A6A5Q0P3) Proteasome subunit beta type-7 × 2 (P30657) Proteasome endopeptidase complex × 2 (A0A6L0ZSP2) MG MAGNESIUM ION × 8 CL CHLORIDE ION × 2 V08 (2 {R},3 {S})-3-methanoyl-4-methyl-2-hydroxy-pentanoic acid × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 3.00 Å R-free 0.216

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q273_YEASX
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–254; UniProt 1–254 Author chain Q; PDBConstruct 1–254; UniProt 1–254

20S proteasome

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain D; UniProt 1–260 Chain R; UniProt 1–260 Not recorded HLJ1_G0039880.mRNA.1.CDS.1 × 2 (A0A6L1BIF8) BJ4_G0021480.mRNA.1.CDS.1 × 2 (A0A6A5PXC6) HLJ1_G0048980.mRNA.1.CDS.1 × 2 (A0A6A5Q273) BJ4_G0043800.mRNA.1.CDS.1 × 2 (A0A6A5PTH4) Probable proteasome subunit alpha type-7 × 2 (A0A6A5Q4M4) BJ4_G0020160.mRNA.1.CDS.1 × 2 (A0A6A5PYC9) Proteasome endopeptidase complex × 2 (A0A6A5Q449) Proteasome endopeptidase complex × 2 (A0A6L0YA22) Proteasome subunit beta × 2 (A0A6A5Q0W2) Proteasome subunit beta type-5 × 2 (A0A6V8RU78) Proteasome endopeptidase complex × 2 (A0A6A5Q0P3) Proteasome subunit beta type-7 × 2 (P30657) Proteasome endopeptidase complex × 2 (A0A6L0ZSP2) MG MAGNESIUM ION × 8 CL CHLORIDE ION × 2 V08 (2 {R},3 {S})-3-methanoyl-4-methyl-2-hydroxy-pentanoic acid × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 3.00 Å R-free 0.216

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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–260; UniProt 1–260 Author chain R; PDBConstruct 1–260; UniProt 1–260

BJ4_G0043800.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A6A5PTH4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain E; UniProt 1–234 Chain S; UniProt 1–234 Not recorded HLJ1_G0039880.mRNA.1.CDS.1 × 2 (A0A6L1BIF8) BJ4_G0021480.mRNA.1.CDS.1 × 2 (A0A6A5PXC6) HLJ1_G0048980.mRNA.1.CDS.1 × 2 (A0A6A5Q273) 20S proteasome × 2 (P32379) Probable proteasome subunit alpha type-7 × 2 (A0A6A5Q4M4) BJ4_G0020160.mRNA.1.CDS.1 × 2 (A0A6A5PYC9) Proteasome endopeptidase complex × 2 (A0A6A5Q449) Proteasome endopeptidase complex × 2 (A0A6L0YA22) Proteasome subunit beta × 2 (A0A6A5Q0W2) Proteasome subunit beta type-5 × 2 (A0A6V8RU78) Proteasome endopeptidase complex × 2 (A0A6A5Q0P3) Proteasome subunit beta type-7 × 2 (P30657) Proteasome endopeptidase complex × 2 (A0A6L0ZSP2) MG MAGNESIUM ION × 8 CL CHLORIDE ION × 2 V08 (2 {R},3 {S})-3-methanoyl-4-methyl-2-hydroxy-pentanoic acid × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 3.00 Å R-free 0.216

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5PTH4_YEASX
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–234; UniProt 1–234 Author chain S; PDBConstruct 1–234; UniProt 1–234

Probable proteasome subunit alpha type-7

OrganismNot specified

UniProt A0A6A5Q4M4

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain F; UniProt 1–288 Chain T; UniProt 1–288 Not recorded HLJ1_G0039880.mRNA.1.CDS.1 × 2 (A0A6L1BIF8) BJ4_G0021480.mRNA.1.CDS.1 × 2 (A0A6A5PXC6) HLJ1_G0048980.mRNA.1.CDS.1 × 2 (A0A6A5Q273) 20S proteasome × 2 (P32379) BJ4_G0043800.mRNA.1.CDS.1 × 2 (A0A6A5PTH4) BJ4_G0020160.mRNA.1.CDS.1 × 2 (A0A6A5PYC9) Proteasome endopeptidase complex × 2 (A0A6A5Q449) Proteasome endopeptidase complex × 2 (A0A6L0YA22) Proteasome subunit beta × 2 (A0A6A5Q0W2) Proteasome subunit beta type-5 × 2 (A0A6V8RU78) Proteasome endopeptidase complex × 2 (A0A6A5Q0P3) Proteasome subunit beta type-7 × 2 (P30657) Proteasome endopeptidase complex × 2 (A0A6L0ZSP2) MG MAGNESIUM ION × 8 CL CHLORIDE ION × 2 V08 (2 {R},3 {S})-3-methanoyl-4-methyl-2-hydroxy-pentanoic acid × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 3.00 Å R-free 0.216

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q4M4_YEASX
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–288; UniProt 1–288 Author chain T; PDBConstruct 1–288; UniProt 1–288

BJ4_G0020160.mRNA.1.CDS.1

OrganismNot specified

UniProt A0A6A5PYC9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain G; UniProt 1–252 Chain U; UniProt 1–252 Not recorded HLJ1_G0039880.mRNA.1.CDS.1 × 2 (A0A6L1BIF8) BJ4_G0021480.mRNA.1.CDS.1 × 2 (A0A6A5PXC6) HLJ1_G0048980.mRNA.1.CDS.1 × 2 (A0A6A5Q273) 20S proteasome × 2 (P32379) BJ4_G0043800.mRNA.1.CDS.1 × 2 (A0A6A5PTH4) Probable proteasome subunit alpha type-7 × 2 (A0A6A5Q4M4) Proteasome endopeptidase complex × 2 (A0A6A5Q449) Proteasome endopeptidase complex × 2 (A0A6L0YA22) Proteasome subunit beta × 2 (A0A6A5Q0W2) Proteasome subunit beta type-5 × 2 (A0A6V8RU78) Proteasome endopeptidase complex × 2 (A0A6A5Q0P3) Proteasome subunit beta type-7 × 2 (P30657) Proteasome endopeptidase complex × 2 (A0A6L0ZSP2) MG MAGNESIUM ION × 8 CL CHLORIDE ION × 2 V08 (2 {R},3 {S})-3-methanoyl-4-methyl-2-hydroxy-pentanoic acid × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 3.00 Å R-free 0.216

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5PYC9_YEASX
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–252; UniProt 1–252 Author chain U; PDBConstruct 1–252; UniProt 1–252

Proteasome endopeptidase complex

OrganismNot specified

UniProt A0A6A5Q449

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain H; UniProt 30–261 Chain V; UniProt 30–261 Not recorded HLJ1_G0039880.mRNA.1.CDS.1 × 2 (A0A6L1BIF8) BJ4_G0021480.mRNA.1.CDS.1 × 2 (A0A6A5PXC6) HLJ1_G0048980.mRNA.1.CDS.1 × 2 (A0A6A5Q273) 20S proteasome × 2 (P32379) BJ4_G0043800.mRNA.1.CDS.1 × 2 (A0A6A5PTH4) Probable proteasome subunit alpha type-7 × 2 (A0A6A5Q4M4) BJ4_G0020160.mRNA.1.CDS.1 × 2 (A0A6A5PYC9) Proteasome endopeptidase complex × 2 (A0A6L0YA22) Proteasome subunit beta × 2 (A0A6A5Q0W2) Proteasome subunit beta type-5 × 2 (A0A6V8RU78) Proteasome endopeptidase complex × 2 (A0A6A5Q0P3) Proteasome subunit beta type-7 × 2 (P30657) Proteasome endopeptidase complex × 2 (A0A6L0ZSP2) MG MAGNESIUM ION × 8 CL CHLORIDE ION × 2 V08 (2 {R},3 {S})-3-methanoyl-4-methyl-2-hydroxy-pentanoic acid × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 3.00 Å R-free 0.216

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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q449_YEASX
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–232; UniProt 30–261 Author chain V; PDBConstruct 1–232; UniProt 30–261

Proteasome endopeptidase complex

OrganismNot specified

UniProt A0A6L0YA22

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain I; UniProt 1–205 Chain W; UniProt 1–205 Not recorded HLJ1_G0039880.mRNA.1.CDS.1 × 2 (A0A6L1BIF8) BJ4_G0021480.mRNA.1.CDS.1 × 2 (A0A6A5PXC6) HLJ1_G0048980.mRNA.1.CDS.1 × 2 (A0A6A5Q273) 20S proteasome × 2 (P32379) BJ4_G0043800.mRNA.1.CDS.1 × 2 (A0A6A5PTH4) Probable proteasome subunit alpha type-7 × 2 (A0A6A5Q4M4) BJ4_G0020160.mRNA.1.CDS.1 × 2 (A0A6A5PYC9) Proteasome endopeptidase complex × 2 (A0A6A5Q449) Proteasome subunit beta × 2 (A0A6A5Q0W2) Proteasome subunit beta type-5 × 2 (A0A6V8RU78) Proteasome endopeptidase complex × 2 (A0A6A5Q0P3) Proteasome subunit beta type-7 × 2 (P30657) Proteasome endopeptidase complex × 2 (A0A6L0ZSP2) MG MAGNESIUM ION × 8 CL CHLORIDE ION × 2 V08 (2 {R},3 {S})-3-methanoyl-4-methyl-2-hydroxy-pentanoic acid × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 3.00 Å R-free 0.216

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6L0YA22_YEASX
Isoform
PDB entities 9
Chains and sequence ranges Author chain I; PDBConstruct 1–205; UniProt 1–205 Author chain W; PDBConstruct 1–205; UniProt 1–205

Proteasome subunit beta

OrganismNot specified

UniProt A0A6A5Q0W2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain J; UniProt 1–198 Chain X; UniProt 1–198 Not recorded HLJ1_G0039880.mRNA.1.CDS.1 × 2 (A0A6L1BIF8) BJ4_G0021480.mRNA.1.CDS.1 × 2 (A0A6A5PXC6) HLJ1_G0048980.mRNA.1.CDS.1 × 2 (A0A6A5Q273) 20S proteasome × 2 (P32379) BJ4_G0043800.mRNA.1.CDS.1 × 2 (A0A6A5PTH4) Probable proteasome subunit alpha type-7 × 2 (A0A6A5Q4M4) BJ4_G0020160.mRNA.1.CDS.1 × 2 (A0A6A5PYC9) Proteasome endopeptidase complex × 2 (A0A6A5Q449) Proteasome endopeptidase complex × 2 (A0A6L0YA22) Proteasome subunit beta type-5 × 2 (A0A6V8RU78) Proteasome endopeptidase complex × 2 (A0A6A5Q0P3) Proteasome subunit beta type-7 × 2 (P30657) Proteasome endopeptidase complex × 2 (A0A6L0ZSP2) MG MAGNESIUM ION × 8 CL CHLORIDE ION × 2 V08 (2 {R},3 {S})-3-methanoyl-4-methyl-2-hydroxy-pentanoic acid × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 3.00 Å R-free 0.216

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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q0W2_YEASX
Isoform
PDB entities 10
Chains and sequence ranges Author chain J; PDBConstruct 1–198; UniProt 1–198 Author chain X; PDBConstruct 1–198; UniProt 1–198

Proteasome subunit beta type-5

OrganismNot specified

UniProt A0A6V8RU78

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain K; UniProt 76–287 Chain Y; UniProt 76–287 Not recorded HLJ1_G0039880.mRNA.1.CDS.1 × 2 (A0A6L1BIF8) BJ4_G0021480.mRNA.1.CDS.1 × 2 (A0A6A5PXC6) HLJ1_G0048980.mRNA.1.CDS.1 × 2 (A0A6A5Q273) 20S proteasome × 2 (P32379) BJ4_G0043800.mRNA.1.CDS.1 × 2 (A0A6A5PTH4) Probable proteasome subunit alpha type-7 × 2 (A0A6A5Q4M4) BJ4_G0020160.mRNA.1.CDS.1 × 2 (A0A6A5PYC9) Proteasome endopeptidase complex × 2 (A0A6A5Q449) Proteasome endopeptidase complex × 2 (A0A6L0YA22) Proteasome subunit beta × 2 (A0A6A5Q0W2) Proteasome endopeptidase complex × 2 (A0A6A5Q0P3) Proteasome subunit beta type-7 × 2 (P30657) Proteasome endopeptidase complex × 2 (A0A6L0ZSP2) MG MAGNESIUM ION × 8 CL CHLORIDE ION × 2 V08 (2 {R},3 {S})-3-methanoyl-4-methyl-2-hydroxy-pentanoic acid × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 3.00 Å R-free 0.216

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 A0A6V8RU78_YEASX
Isoform
PDB entities 11
Chains and sequence ranges Author chain K; PDBConstruct 1–212; UniProt 76–287 Author chain Y; PDBConstruct 1–212; UniProt 76–287

Proteasome endopeptidase complex

OrganismNot specified

UniProt A0A6A5Q0P3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain L; UniProt 20–241 Chain Z; UniProt 20–241 Not recorded HLJ1_G0039880.mRNA.1.CDS.1 × 2 (A0A6L1BIF8) BJ4_G0021480.mRNA.1.CDS.1 × 2 (A0A6A5PXC6) HLJ1_G0048980.mRNA.1.CDS.1 × 2 (A0A6A5Q273) 20S proteasome × 2 (P32379) BJ4_G0043800.mRNA.1.CDS.1 × 2 (A0A6A5PTH4) Probable proteasome subunit alpha type-7 × 2 (A0A6A5Q4M4) BJ4_G0020160.mRNA.1.CDS.1 × 2 (A0A6A5PYC9) Proteasome endopeptidase complex × 2 (A0A6A5Q449) Proteasome endopeptidase complex × 2 (A0A6L0YA22) Proteasome subunit beta × 2 (A0A6A5Q0W2) Proteasome subunit beta type-5 × 2 (A0A6V8RU78) Proteasome subunit beta type-7 × 2 (P30657) Proteasome endopeptidase complex × 2 (A0A6L0ZSP2) MG MAGNESIUM ION × 8 CL CHLORIDE ION × 2 V08 (2 {R},3 {S})-3-methanoyl-4-methyl-2-hydroxy-pentanoic acid × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 3.00 Å R-free 0.216

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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A6A5Q0P3_YEASX
Isoform
PDB entities 12
Chains and sequence ranges Author chain L; PDBConstruct 1–222; UniProt 20–241 Author chain Z; PDBConstruct 1–222; UniProt 20–241

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain M; UniProt 21–266 Chain a; UniProt 21–266 Not recorded HLJ1_G0039880.mRNA.1.CDS.1 × 2 (A0A6L1BIF8) BJ4_G0021480.mRNA.1.CDS.1 × 2 (A0A6A5PXC6) HLJ1_G0048980.mRNA.1.CDS.1 × 2 (A0A6A5Q273) 20S proteasome × 2 (P32379) BJ4_G0043800.mRNA.1.CDS.1 × 2 (A0A6A5PTH4) Probable proteasome subunit alpha type-7 × 2 (A0A6A5Q4M4) BJ4_G0020160.mRNA.1.CDS.1 × 2 (A0A6A5PYC9) Proteasome endopeptidase complex × 2 (A0A6A5Q449) Proteasome endopeptidase complex × 2 (A0A6L0YA22) Proteasome subunit beta × 2 (A0A6A5Q0W2) Proteasome subunit beta type-5 × 2 (A0A6V8RU78) Proteasome endopeptidase complex × 2 (A0A6A5Q0P3) Proteasome endopeptidase complex × 2 (A0A6L0ZSP2) MG MAGNESIUM ION × 8 CL CHLORIDE ION × 2 V08 (2 {R},3 {S})-3-methanoyl-4-methyl-2-hydroxy-pentanoic acid × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 3.00 Å R-free 0.216

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 13
Chains and sequence ranges Author chain M; PDBConstruct 1–246; UniProt 21–266 Author chain a; PDBConstruct 1–246; UniProt 21–266

Proteasome endopeptidase complex

OrganismNot specified

UniProt A0A6L0ZSP2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain N; UniProt 20–215 Chain b; UniProt 20–215 Not recorded HLJ1_G0039880.mRNA.1.CDS.1 × 2 (A0A6L1BIF8) BJ4_G0021480.mRNA.1.CDS.1 × 2 (A0A6A5PXC6) HLJ1_G0048980.mRNA.1.CDS.1 × 2 (A0A6A5Q273) 20S proteasome × 2 (P32379) BJ4_G0043800.mRNA.1.CDS.1 × 2 (A0A6A5PTH4) Probable proteasome subunit alpha type-7 × 2 (A0A6A5Q4M4) BJ4_G0020160.mRNA.1.CDS.1 × 2 (A0A6A5PYC9) Proteasome endopeptidase complex × 2 (A0A6A5Q449) Proteasome endopeptidase complex × 2 (A0A6L0YA22) Proteasome subunit beta × 2 (A0A6A5Q0W2) Proteasome subunit beta type-5 × 2 (A0A6V8RU78) Proteasome endopeptidase complex × 2 (A0A6A5Q0P3) Proteasome subunit beta type-7 × 2 (P30657) MG MAGNESIUM ION × 8 CL CHLORIDE ION × 2 V08 (2 {R},3 {S})-3-methanoyl-4-methyl-2-hydroxy-pentanoic acid × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 3.00 Å R-free 0.216

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 A0A6L0ZSP2_YEASX
Isoform
PDB entities 14
Chains and sequence ranges Author chain N; PDBConstruct 1–196; UniProt 20–215 Author chain b; PDBConstruct 1–196; UniProt 20–215

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 7o2l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7o2l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7o2l
Deposition date deposition_date2021-03-30
Structure title titleYeast 20S proteasome in complex with the covalently bound inhibitor b-lactone (2R,3S)-3-isopropyl-4-oxo-2-oxetane-carboxylate (IOC)
Keywords keywordsHYDROLASE-HYDROLASE INHIBITOR complex, Proteasome, b-lactone, Binding Analysis, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier60.42
Radius of gyration Rg (electron density) rg_electron59.96
Forward intensity I(0) i06788000000.00
Molecular weight molecular_weight700790.0 kDa
Excluded volume excluded_volume878950 ų
Envelope volume envelope_volume1266200 ų
Hydration-shell volume shell_volume169430 ų
Envelope diameter envelope_diameter195.2
Shell Rg shell_rg68.02
Envelope Rg envelope_rg57.83
Shape Rg shape_rg59.95
Total Rg total_rg60.17
Total atoms total_atoms49366
Residues n_residues6334
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 dmax194.9
Rg (real space) rg_real60.14
Rg uncertainty (real space) rg_real_error1.68
I(0) (real space) i0_real6.7880e+09
I(0) uncertainty (real space) i0_real_error1.4010e+08
Rg (reciprocal space) rg_reciprocal60.64
I(0) (reciprocal space) i0_reciprocal6793000000.0000
Solution quality estimate total_estimate0.7981
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary75.0
Skewness Skewness skewness0.208
Kurtosis Kurtosis kurtosis-0.419
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1076000000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.805; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.956; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (18)

7. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

Domain ID domain_id7o2lA01
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_id7o2lB01
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_id7o2lC01
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_id7o2lD01
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_id7o2lF01
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_id7o2lH01
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_id7o2lK01
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_id7o2lL01
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_id7o2lO01
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_id7o2lP01
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_id7o2lQ01
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_id7o2lR01
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_id7o2lT01
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_id7o2lV01
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_id7o2lY01
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_id7o2lZ01
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

8. Citations (1)

9. Files and Curves (10)