7awe

HUMAN IMMUNOPROTEASOME 20S PARTICLE IN COMPLEX WITH [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid

Method: X-RAY DIFFRACTION Dmax: 196.8 Å Quality: GOOD

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

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain A; UniProt 4–245 Chain O; UniProt 4–245 Fragment:20S CORE 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-9 × 2 (P28065) Proteasome subunit beta type-10 × 2 (P40306) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-8 × 2 (P28062) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) NA SODIUM ION × 13 SCN THIOCYANATE ION × 11 S5K [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;42 % MPD, 0.20 M NaSCN Resolution 2.29 Å R-free 0.214

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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–242; UniProt 4–245 Author chain O; PDBConstruct 1–242; UniProt 4–245

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain B; UniProt 5–233 Chain P; UniProt 5–233 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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-9 × 2 (P28065) Proteasome subunit beta type-10 × 2 (P40306) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-8 × 2 (P28062) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) NA SODIUM ION × 13 SCN THIOCYANATE ION × 11 S5K [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;42 % MPD, 0.20 M NaSCN Resolution 2.29 Å R-free 0.214

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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–229; UniProt 5–233 Author chain P; PDBConstruct 1–229; UniProt 5–233

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain C; UniProt 2–257 Chain Q; UniProt 2–257 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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 beta type-9 × 2 (P28065) Proteasome subunit beta type-10 × 2 (P40306) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-8 × 2 (P28062) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) NA SODIUM ION × 13 SCN THIOCYANATE ION × 11 S5K [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;42 % MPD, 0.20 M NaSCN Resolution 2.29 Å R-free 0.214

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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–256; UniProt 2–257 Author chain Q; PDBConstruct 1–256; UniProt 2–257

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain D; UniProt 2–238 Chain R; UniProt 2–238 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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 beta type-9 × 2 (P28065) Proteasome subunit beta type-10 × 2 (P40306) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-8 × 2 (P28062) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) NA SODIUM ION × 13 SCN THIOCYANATE ION × 11 S5K [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;42 % MPD, 0.20 M NaSCN Resolution 2.29 Å R-free 0.214

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 4
Chains and sequence ranges Author chain D; PDBConstruct 1–237; UniProt 2–238 Author chain R; PDBConstruct 1–237; UniProt 2–238

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain E; UniProt 9–240 Chain S; UniProt 9–240 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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 beta type-9 × 2 (P28065) Proteasome subunit beta type-10 × 2 (P40306) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-8 × 2 (P28062) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) NA SODIUM ION × 13 SCN THIOCYANATE ION × 11 S5K [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;42 % MPD, 0.20 M NaSCN Resolution 2.29 Å R-free 0.214

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 5
Chains and sequence ranges Author chain E; PDBConstruct 1–232; UniProt 9–240 Author chain S; PDBConstruct 1–232; UniProt 9–240

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain F; UniProt 4–239 Chain T; UniProt 4–239 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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 beta type-9 × 2 (P28065) Proteasome subunit beta type-10 × 2 (P40306) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-8 × 2 (P28062) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) NA SODIUM ION × 13 SCN THIOCYANATE ION × 11 S5K [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;42 % MPD, 0.20 M NaSCN Resolution 2.29 Å R-free 0.214

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 6
Chains and sequence ranges Author chain F; PDBConstruct 1–236; UniProt 4–239 Author chain T; PDBConstruct 1–236; UniProt 4–239

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain G; UniProt 5–246 Chain U; UniProt 5–246 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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 beta type-9 × 2 (P28065) Proteasome subunit beta type-10 × 2 (P40306) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-8 × 2 (P28062) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) NA SODIUM ION × 13 SCN THIOCYANATE ION × 11 S5K [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;42 % MPD, 0.20 M NaSCN Resolution 2.29 Å R-free 0.214

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 7
Chains and sequence ranges Author chain G; PDBConstruct 1–242; UniProt 5–246 Author chain U; PDBConstruct 1–242; UniProt 5–246

Proteasome subunit beta type-9

OrganismNot specified

UniProt P28065

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 21–219 Chain V; UniProt 21–219 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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-10 × 2 (P40306) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-8 × 2 (P28062) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) NA SODIUM ION × 13 SCN THIOCYANATE ION × 11 S5K [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;42 % MPD, 0.20 M NaSCN Resolution 2.29 Å R-free 0.214

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 PSB9_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–199; UniProt 21–219 Author chain V; PDBConstruct 1–199; UniProt 21–219

Proteasome subunit beta type-10

OrganismNot specified

UniProt P40306

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 40–262 Chain W; UniProt 40–262 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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-9 × 2 (P28065) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-8 × 2 (P28062) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) NA SODIUM ION × 13 SCN THIOCYANATE ION × 11 S5K [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;42 % MPD, 0.20 M NaSCN Resolution 2.29 Å R-free 0.214

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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB10_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain I; PDBConstruct 1–223; UniProt 40–262 Author chain W; PDBConstruct 1–223; UniProt 40–262

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain J; UniProt 2–205 Chain X; UniProt 2–205 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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-9 × 2 (P28065) Proteasome subunit beta type-10 × 2 (P40306) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-8 × 2 (P28062) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) NA SODIUM ION × 13 SCN THIOCYANATE ION × 11 S5K [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;42 % MPD, 0.20 M NaSCN Resolution 2.29 Å R-free 0.214

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 10
Chains and sequence ranges Author chain J; PDBConstruct 1–204; UniProt 2–205 Author chain X; PDBConstruct 1–204; UniProt 2–205

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain K; UniProt 1–197 Chain Y; UniProt 1–197 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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-9 × 2 (P28065) Proteasome subunit beta type-10 × 2 (P40306) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-8 × 2 (P28062) Proteasome subunit beta type-1 × 2 (P20618) Proteasome subunit beta type-4 × 2 (P28070) NA SODIUM ION × 13 SCN THIOCYANATE ION × 11 S5K [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;42 % MPD, 0.20 M NaSCN Resolution 2.29 Å R-free 0.214

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 11
Chains and sequence ranges Author chain K; PDBConstruct 1–197; UniProt 1–197 Author chain Y; PDBConstruct 1–197; UniProt 1–197

Proteasome subunit beta type-8

OrganismNot specified

UniProt P28062

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 73–275 Chain Z; UniProt 73–275 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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-9 × 2 (P28065) Proteasome subunit beta type-10 × 2 (P40306) 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) NA SODIUM ION × 13 SCN THIOCYANATE ION × 11 S5K [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;42 % MPD, 0.20 M NaSCN Resolution 2.29 Å R-free 0.214

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.

21 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB8_HUMAN
Isoform
PDB entities 12
Chains and sequence ranges Author chain L; PDBConstruct 1–203; UniProt 73–275 Author chain Z; PDBConstruct 1–203; UniProt 73–275

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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain M; UniProt 29–241 Chain a; UniProt 29–241 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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-9 × 2 (P28065) Proteasome subunit beta type-10 × 2 (P40306) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-8 × 2 (P28062) Proteasome subunit beta type-4 × 2 (P28070) NA SODIUM ION × 13 SCN THIOCYANATE ION × 11 S5K [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;42 % MPD, 0.20 M NaSCN Resolution 2.29 Å R-free 0.214

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 13
Chains and sequence ranges Author chain M; PDBConstruct 1–213; UniProt 29–241 Author chain a; 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 × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain N; UniProt 46–259 Chain b; UniProt 46–259 Not recorded Proteasome subunit alpha type-6 × 2 (P60900) 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-9 × 2 (P28065) Proteasome subunit beta type-10 × 2 (P40306) Proteasome subunit beta type-3 × 2 (P49720) Proteasome subunit beta type-2 × 2 (P49721) Proteasome subunit beta type-8 × 2 (P28062) Proteasome subunit beta type-1 × 2 (P20618) NA SODIUM ION × 13 SCN THIOCYANATE ION × 11 S5K [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.6;291 K;42 % MPD, 0.20 M NaSCN Resolution 2.29 Å R-free 0.214

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 14
Chains and sequence ranges Author chain N; PDBConstruct 1–214; UniProt 46–259 Author chain b; PDBConstruct 1–214; UniProt 46–259

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 7awe

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7awe
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7awe
Deposition date deposition_date2020-11-06
Structure title titleHUMAN IMMUNOPROTEASOME 20S PARTICLE IN COMPLEX WITH [(1R)-2-(1-benzofuran-3-yl)-1-{[(1S,2R,4R)-7-oxabicyclo[2.2.1]heptan-2-yl]formamido}ethyl]boronic acid
Keywords keywordsMULTICATALYTIC PROTEINASE, 20S PROTEASOME, PROTEASE, HYDROLASE, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier60.12
Radius of gyration Rg (electron density) rg_electron59.79
Forward intensity I(0) i06661600000.00
Molecular weight molecular_weight690220.0 kDa
Excluded volume excluded_volume864200 ų
Envelope volume envelope_volume1245900 ų
Hydration-shell volume shell_volume167170 ų
Envelope diameter envelope_diameter204.2
Shell Rg shell_rg67.55
Envelope Rg envelope_rg57.93
Shape Rg shape_rg59.78
Total Rg total_rg59.97
Total atoms total_atoms48444
Residues n_residues6217
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 dmax196.8
Rg (real space) rg_real59.85
Rg uncertainty (real space) rg_real_error1.50
I(0) (real space) i0_real6.6620e+09
I(0) uncertainty (real space) i0_real_error1.3890e+08
Rg (reciprocal space) rg_reciprocal60.32
I(0) (reciprocal space) i0_reciprocal6667000000.0000
Solution quality estimate total_estimate0.8564
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary75.7
Skewness Skewness skewness0.220
Kurtosis Kurtosis kurtosis-0.400
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha951900000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.779; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.954; Smooth: 0.837

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (18)

7. Fold Classification (SCOP + CATH) 39 domains

SCOP 2.08 (25 domains)

Domain ID domain_idd7awea_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7aweb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.0 — automated matches
Domain ID domain_idd7awec_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.0 — automated matches
Domain ID domain_idd7awed_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7awee_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7awef_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7aweg_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7aweh_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.0 — automated matches
Domain ID domain_idd7awei_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7awej_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7awek_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7awel_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7awem_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7awen_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.0 — automated matches
Domain ID domain_idd7aweo_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7awep_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7awer_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7awes_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7awet_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7aweu_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7awev_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.0 — automated matches
Domain ID domain_idd7awew_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7awex_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7awey_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits
Domain ID domain_idd7awez_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.153 — Ntn hydrolase-like
Superfamily Superfamily superfamilyd.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family familyd.153.1.4 — Proteasome subunits

CATH v4.4 (14 domains)

Domain ID domain_id7aweB01
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_id7aweC01
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_id7aweD01
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_id7aweE01
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_id7aweI01
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_id7aweL01
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_id7aweM01
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_id7aweP01
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_id7aweQ01
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_id7aweR01
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_id7aweS01
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_id7aweW01
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_id7aweZ01
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_id7awea01
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)