5lf0

Human 20S proteasome complex with Epoxomicin at 2.4 Angstrom

Method: X-RAY DIFFRACTION Dmax: 196.1 Å Quality: GOOD

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

Proteasome subunit alpha type-2

OrganismNot specified

UniProt P25787

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain A; UniProt 1–234 Chain O; UniProt 1–234 Not recorded Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) EPOXOMICIN (peptide inhibitor) × 6 CL CHLORIDE ION × 58 K POTASSIUM ION × 6 MG MAGNESIUM ION × 10 1PE PENTAETHYLENE GLYCOL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M Bis-Tris, 0.2 M Magnesium Chloride, 10 % PEG3350 Resolution 2.41 Å R-free 0.229

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.

170 other PDB entries and 171 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–234; UniProt 1–234 Author chain O; PDBConstruct 1–234; UniProt 1–234

Proteasome subunit alpha type-4

OrganismNot specified

UniProt P25789

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain B; UniProt 1–261 Chain P; UniProt 1–261 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) EPOXOMICIN (peptide inhibitor) × 6 CL CHLORIDE ION × 58 K POTASSIUM ION × 6 MG MAGNESIUM ION × 10 1PE PENTAETHYLENE GLYCOL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M Bis-Tris, 0.2 M Magnesium Chloride, 10 % PEG3350 Resolution 2.41 Å R-free 0.229

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.

170 other PDB entries and 171 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–261; UniProt 1–261 Author chain P; PDBConstruct 1–261; UniProt 1–261

Proteasome subunit alpha type-7

OrganismNot specified

UniProt O14818

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain C; UniProt 1–248 Chain Q; UniProt 1–248 Non-standard monomer:Yes (specific site not provided by mmCIF) Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) EPOXOMICIN (peptide inhibitor) × 6 CL CHLORIDE ION × 58 K POTASSIUM ION × 6 MG MAGNESIUM ION × 10 1PE PENTAETHYLENE GLYCOL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M Bis-Tris, 0.2 M Magnesium Chloride, 10 % PEG3350 Resolution 2.41 Å R-free 0.229

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.

170 other PDB entries and 171 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA7_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–248; UniProt 1–248 Author chain Q; PDBConstruct 1–248; UniProt 1–248

Proteasome subunit alpha type-5

OrganismNot specified

UniProt P28066

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain D; UniProt 1–241 Chain R; UniProt 1–241 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) EPOXOMICIN (peptide inhibitor) × 6 CL CHLORIDE ION × 58 K POTASSIUM ION × 6 MG MAGNESIUM ION × 10 1PE PENTAETHYLENE GLYCOL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M Bis-Tris, 0.2 M Magnesium Chloride, 10 % PEG3350 Resolution 2.41 Å R-free 0.229

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.

170 other PDB entries and 171 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA5_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–241; UniProt 1–241 Author chain R; PDBConstruct 1–241; UniProt 1–241

Proteasome subunit alpha type-1

OrganismNot specified

UniProt P25786

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain E; UniProt 1–263 Chain S; UniProt 1–263 Non-standard monomer:Yes (specific site not provided by mmCIF) Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) EPOXOMICIN (peptide inhibitor) × 6 CL CHLORIDE ION × 58 K POTASSIUM ION × 6 MG MAGNESIUM ION × 10 1PE PENTAETHYLENE GLYCOL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M Bis-Tris, 0.2 M Magnesium Chloride, 10 % PEG3350 Resolution 2.41 Å R-free 0.229

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.

170 other PDB entries and 171 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA1_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–263; UniProt 1–263 Author chain S; PDBConstruct 1–263; UniProt 1–263

Proteasome subunit alpha type-3

OrganismNot specified

UniProt P25788

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain F; UniProt 1–255 Chain T; UniProt 1–255 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) EPOXOMICIN (peptide inhibitor) × 6 CL CHLORIDE ION × 58 K POTASSIUM ION × 6 MG MAGNESIUM ION × 10 1PE PENTAETHYLENE GLYCOL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M Bis-Tris, 0.2 M Magnesium Chloride, 10 % PEG3350 Resolution 2.41 Å R-free 0.229

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.

172 other PDB entries and 175 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA3_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–255; UniProt 1–255 Author chain T; PDBConstruct 1–255; UniProt 1–255

Proteasome subunit alpha type-6

OrganismNot specified

UniProt P60900

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain G; UniProt 1–246 Chain U; UniProt 1–246 Non-standard monomer:Yes (specific site not provided by mmCIF) Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) EPOXOMICIN (peptide inhibitor) × 6 CL CHLORIDE ION × 58 K POTASSIUM ION × 6 MG MAGNESIUM ION × 10 1PE PENTAETHYLENE GLYCOL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M Bis-Tris, 0.2 M Magnesium Chloride, 10 % PEG3350 Resolution 2.41 Å R-free 0.229

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.

170 other PDB entries and 171 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA6_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–246; UniProt 1–246 Author chain U; PDBConstruct 1–246; UniProt 1–246

Proteasome subunit beta type-7

OrganismNot specified

UniProt Q99436

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain H; UniProt 44–277 Chain V; UniProt 44–277 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) EPOXOMICIN (peptide inhibitor) × 6 CL CHLORIDE ION × 58 K POTASSIUM ION × 6 MG MAGNESIUM ION × 10 1PE PENTAETHYLENE GLYCOL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M Bis-Tris, 0.2 M Magnesium Chloride, 10 % PEG3350 Resolution 2.41 Å R-free 0.229

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.

159 other PDB entries and 160 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB7_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–234; UniProt 44–277 Author chain V; PDBConstruct 1–234; UniProt 44–277

Proteasome subunit beta type-3

OrganismNot specified

UniProt P49720

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain I; UniProt 1–205 Chain W; UniProt 1–205 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) EPOXOMICIN (peptide inhibitor) × 6 CL CHLORIDE ION × 58 K POTASSIUM ION × 6 MG MAGNESIUM ION × 10 1PE PENTAETHYLENE GLYCOL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M Bis-Tris, 0.2 M Magnesium Chloride, 10 % PEG3350 Resolution 2.41 Å R-free 0.229

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.

150 other PDB entries and 151 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB3_HUMAN
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 type-2

OrganismNot specified

UniProt P49721

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain J; UniProt 1–201 Chain X; UniProt 1–201 Non-standard monomer:Yes (specific site not provided by mmCIF) Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) EPOXOMICIN (peptide inhibitor) × 6 CL CHLORIDE ION × 58 K POTASSIUM ION × 6 MG MAGNESIUM ION × 10 1PE PENTAETHYLENE GLYCOL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M Bis-Tris, 0.2 M Magnesium Chloride, 10 % PEG3350 Resolution 2.41 Å R-free 0.229

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.

149 other PDB entries and 150 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB2_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain J; PDBConstruct 1–201; UniProt 1–201 Author chain X; PDBConstruct 1–201; UniProt 1–201

Proteasome subunit beta type-5

OrganismNot specified

UniProt P28074

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain K; UniProt 60–263 Chain Y; UniProt 60–263 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) EPOXOMICIN (peptide inhibitor) × 6 CL CHLORIDE ION × 58 K POTASSIUM ION × 6 MG MAGNESIUM ION × 10 1PE PENTAETHYLENE GLYCOL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M Bis-Tris, 0.2 M Magnesium Chloride, 10 % PEG3350 Resolution 2.41 Å R-free 0.229

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.

151 other PDB entries and 152 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB5_HUMAN
Isoform
PDB entities 11
Chains and sequence ranges Author chain K; PDBConstruct 1–204; UniProt 60–263 Author chain Y; PDBConstruct 1–204; UniProt 60–263

Proteasome subunit beta type-1

OrganismNot specified

UniProt P20618

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain L; UniProt 29–241 Chain Z; UniProt 29–241 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-4 × 2 (P28070) Proteasome subunit beta type-6 × 2 (P28072) EPOXOMICIN (peptide inhibitor) × 6 CL CHLORIDE ION × 58 K POTASSIUM ION × 6 MG MAGNESIUM ION × 10 1PE PENTAETHYLENE GLYCOL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M Bis-Tris, 0.2 M Magnesium Chloride, 10 % PEG3350 Resolution 2.41 Å R-free 0.229

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.

170 other PDB entries and 171 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB1_HUMAN
Isoform
PDB entities 12
Chains and sequence ranges Author chain L; PDBConstruct 1–213; UniProt 29–241 Author chain Z; PDBConstruct 1–213; UniProt 29–241

Proteasome subunit beta type-4

OrganismNot specified

UniProt P28070

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain M; UniProt 46–264 Chain a; UniProt 46–264 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-6 × 2 (P28072) EPOXOMICIN (peptide inhibitor) × 6 CL CHLORIDE ION × 58 K POTASSIUM ION × 6 MG MAGNESIUM ION × 10 1PE PENTAETHYLENE GLYCOL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M Bis-Tris, 0.2 M Magnesium Chloride, 10 % PEG3350 Resolution 2.41 Å R-free 0.229

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.

145 other PDB entries and 146 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB4_HUMAN
Isoform
PDB entities 13
Chains and sequence ranges Author chain M; PDBConstruct 1–219; UniProt 46–264 Author chain a; PDBConstruct 1–219; UniProt 46–264

Proteasome subunit beta type-6

OrganismNot specified

UniProt P28072

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 34 PDB declaration: 34-meric(34) Consistent with protein copy count Chain N; UniProt 35–239 Chain b; UniProt 35–239 Not recorded Proteasome subunit alpha type-2 × 2 (P25787) Proteasome subunit alpha type-4 × 2 (P25789) Proteasome subunit alpha type-7 × 2 (O14818) Proteasome subunit alpha type-5 × 2 (P28066) Proteasome subunit alpha type-1 × 2 (P25786) Proteasome subunit alpha type-3 × 2 (P25788) Proteasome subunit alpha type-6 × 2 (P60900) Proteasome subunit beta type-7 × 2 (Q99436) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-5 × 2 (P28074) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) EPOXOMICIN (peptide inhibitor) × 6 CL CHLORIDE ION × 58 K POTASSIUM ION × 6 MG MAGNESIUM ION × 10 1PE PENTAETHYLENE GLYCOL × 9 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;291 K;0.1 M Bis-Tris, 0.2 M Magnesium Chloride, 10 % PEG3350 Resolution 2.41 Å R-free 0.229

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.

141 other PDB entries and 142 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB6_HUMAN
Isoform
PDB entities 14
Chains and sequence ranges Author chain N; PDBConstruct 1–205; UniProt 35–239 Author chain b; PDBConstruct 1–205; UniProt 35–239

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 5lf0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5lf0
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id5lf0
Deposition date deposition_date2016-06-30
Structure title titleHuman 20S proteasome complex with Epoxomicin at 2.4 Angstrom
Keywords keywordsProteasome, Multicatalytic Proteinase, NTN-Hydrolase, hydrolase; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier59.90
Radius of gyration Rg (electron density) rg_electron59.38
Forward intensity I(0) i06688280000.00
Molecular weight molecular_weight689650.0 kDa
Excluded volume excluded_volume862330 ų
Envelope volume envelope_volume1232000 ų
Hydration-shell volume shell_volume166090 ų
Envelope diameter envelope_diameter202.0
Shell Rg shell_rg67.34
Envelope Rg envelope_rg57.62
Shape Rg shape_rg59.41
Total Rg total_rg59.43
Total atoms total_atoms48324
Residues n_residues6235
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 dmax196.1
Rg (real space) rg_real59.64
Rg uncertainty (real space) rg_real_error1.19
I(0) (real space) i0_real6.6880e+09
I(0) uncertainty (real space) i0_real_error1.2060e+08
Rg (reciprocal space) rg_reciprocal60.10
I(0) (reciprocal space) i0_reciprocal6693000000.0000
Solution quality estimate total_estimate0.8553
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary75.4
Skewness Skewness skewness0.227
Kurtosis Kurtosis kurtosis-0.400
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha879900000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.780; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; Smooth: 0.820

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (20)

7. Fold Classification (SCOP + CATH) 28 domains

CATH v4.4 (28 domains)

Domain ID domain_id5lf0A00
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_id5lf0B00
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_id5lf0C00
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_id5lf0D00
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_id5lf0E00
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_id5lf0F00
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_id5lf0G00
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_id5lf0H00
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_id5lf0I00
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_id5lf0J00
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_id5lf0K00
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_id5lf0L00
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_id5lf0M00
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_id5lf0N00
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_id5lf0O00
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_id5lf0P00
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_id5lf0Q00
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_id5lf0R00
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_id5lf0S00
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_id5lf0T00
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_id5lf0U00
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_id5lf0V00
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_id5lf0W00
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_id5lf0X00
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_id5lf0Y00
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_id5lf0Z00
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_id5lf0a00
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_id5lf0b00
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)