4qwu

yCP beta5-C52F mutant in complex with bortezomib

Method: X-RAY DIFFRACTION Dmax: 189.2 Å Quality: GOOD

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

Proteasome subunit alpha type-2

OrganismNot specified

UniProt P23639

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain A; UniProt 1–250 Chain O; UniProt 1–250 Mutation:C52F Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Probable proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit beta type-1 × 2 (P38624) MG MAGNESIUM ION × 7 CL CHLORIDE ION × 4 BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K Resolution 3.00 Å R-free 0.218

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

373 other PDB entries and 374 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA2_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–250; UniProt 1–250 Author chain O; PDBConstruct 1–250; UniProt 1–250

Proteasome subunit alpha type-3

OrganismNot specified

UniProt P23638

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain B; UniProt 1–258 Chain P; UniProt 1–258 Not recorded Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Probable proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit beta type-1 × 2 (P38624) MG MAGNESIUM ION × 7 CL CHLORIDE ION × 4 BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K Resolution 3.00 Å R-free 0.218

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

371 other PDB entries and 372 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA3_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–258; UniProt 1–258 Author chain P; PDBConstruct 1–258; UniProt 1–258

Proteasome subunit alpha type-4

OrganismNot specified

UniProt P40303

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain C; UniProt 1–254 Chain Q; UniProt 1–254 Not recorded Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Probable proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit beta type-1 × 2 (P38624) MG MAGNESIUM ION × 7 CL CHLORIDE ION × 4 BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K Resolution 3.00 Å R-free 0.218

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

373 other PDB entries and 374 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA4_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–254; UniProt 1–254 Author chain Q; PDBConstruct 1–254; UniProt 1–254

Proteasome subunit alpha type-5

OrganismNot specified

UniProt P32379

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain D; UniProt 1–260 Chain R; UniProt 1–260 Not recorded Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-6 × 2 (P40302) Probable proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit beta type-1 × 2 (P38624) MG MAGNESIUM ION × 7 CL CHLORIDE ION × 4 BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K Resolution 3.00 Å R-free 0.218

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

Proteasome subunit alpha type-6

OrganismNot specified

UniProt P40302

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain E; UniProt 1–234 Chain S; UniProt 1–234 Not recorded Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Probable proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit beta type-1 × 2 (P38624) MG MAGNESIUM ION × 7 CL CHLORIDE ION × 4 BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K Resolution 3.00 Å R-free 0.218

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

371 other PDB entries and 372 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA6_YEAST
Isoform
PDB entities 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 P21242

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain F; UniProt 1–288 Chain T; UniProt 1–288 Not recorded Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit beta type-1 × 2 (P38624) MG MAGNESIUM ION × 7 CL CHLORIDE ION × 4 BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K Resolution 3.00 Å R-free 0.218

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

372 other PDB entries and 373 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA7_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–288; UniProt 1–288 Author chain T; PDBConstruct 1–288; UniProt 1–288

Proteasome subunit alpha type-1

OrganismNot specified

UniProt P21243

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain G; UniProt 1–252 Chain U; UniProt 1–252 Not recorded Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Probable proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit beta type-1 × 2 (P38624) MG MAGNESIUM ION × 7 CL CHLORIDE ION × 4 BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K Resolution 3.00 Å R-free 0.218

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

374 other PDB entries and 375 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSA1_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–252; UniProt 1–252 Author chain U; PDBConstruct 1–252; UniProt 1–252

Proteasome subunit beta type-2

OrganismNot specified

UniProt P25043

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain H; UniProt 30–261 Chain V; UniProt 30–261 Not recorded Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Probable proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit beta type-1 × 2 (P38624) MG MAGNESIUM ION × 7 CL CHLORIDE ION × 4 BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K Resolution 3.00 Å R-free 0.218

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

358 other PDB entries and 359 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB2_YEAST
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–232; UniProt 30–261 Author chain V; PDBConstruct 1–232; UniProt 30–261

Proteasome subunit beta type-3

OrganismNot specified

UniProt P25451

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain I; UniProt 1–205 Chain W; UniProt 1–205 Not recorded Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Probable proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit beta type-1 × 2 (P38624) MG MAGNESIUM ION × 7 CL CHLORIDE ION × 4 BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K Resolution 3.00 Å R-free 0.218

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

369 other PDB entries and 370 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB3_YEAST
Isoform
PDB entities 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-4

OrganismNot specified

UniProt P22141

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain J; UniProt 1–198 Chain X; UniProt 1–198 Not recorded Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Probable proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit beta type-1 × 2 (P38624) MG MAGNESIUM ION × 7 CL CHLORIDE ION × 4 BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K Resolution 3.00 Å R-free 0.218

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

369 other PDB entries and 370 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB4_YEAST
Isoform
PDB entities 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

Saccharomyces cerevisiae

UniProt P30656

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain K; UniProt 76–287 Chain Y; UniProt 76–287 Not recorded Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Probable proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit beta type-1 × 2 (P38624) MG MAGNESIUM ION × 7 CL CHLORIDE ION × 4 BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K Resolution 3.00 Å R-free 0.218

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

360 other PDB entries and 361 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB5_YEAST
Isoform
PDB entities 11
Chains and sequence ranges Author chain K; PDBConstruct 1–212; UniProt 76–287 Author chain Y; PDBConstruct 1–212; UniProt 76–287

Proteasome subunit beta type-6

OrganismNot specified

UniProt P23724

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain L; UniProt 20–241 Chain Z; UniProt 20–241 Not recorded Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Probable proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-7 × 2 (P30657) Proteasome subunit beta type-1 × 2 (P38624) MG MAGNESIUM ION × 7 CL CHLORIDE ION × 4 BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K Resolution 3.00 Å R-free 0.218

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

359 other PDB entries and 360 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB6_YEAST
Isoform
PDB entities 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 Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Probable proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-1 × 2 (P38624) MG MAGNESIUM ION × 7 CL CHLORIDE ION × 4 BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K Resolution 3.00 Å R-free 0.218

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 subunit beta type-1

OrganismNot specified

UniProt P38624

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain N; UniProt 20–215 Chain b; UniProt 20–215 Not recorded Proteasome subunit alpha type-2 × 2 (P23639) Proteasome subunit alpha type-3 × 2 (P23638) Proteasome subunit alpha type-4 × 2 (P40303) Proteasome subunit alpha type-5 × 2 (P32379) Proteasome subunit alpha type-6 × 2 (P40302) Probable proteasome subunit alpha type-7 × 2 (P21242) Proteasome subunit alpha type-1 × 2 (P21243) Proteasome subunit beta type-2 × 2 (P25043) Proteasome subunit beta type-3 × 2 (P25451) Proteasome subunit beta type-4 × 2 (P22141) Proteasome subunit beta type-5 × 2 (P30656) Proteasome subunit beta type-6 × 2 (P23724) Proteasome subunit beta type-7 × 2 (P30657) MG MAGNESIUM ION × 7 CL CHLORIDE ION × 4 BO2 N-[(1R)-1-(DIHYDROXYBORYL)-3-METHYLBUTYL]-N-(PYRAZIN-2-YLCARBONYL)-L-PHENYLALANINAMIDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 MM MGAC2, 13% MPD, PH 6.8, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K Resolution 3.00 Å R-free 0.218

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

365 other PDB entries and 366 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PSB1_YEAST
Isoform
PDB entities 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 4qwu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4qwu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4qwu
Deposition date deposition_date2014-07-17
Structure title titleyCP beta5-C52F mutant in complex with bortezomib
Keywords keywordsCancer, Proteasome, Bortezomib, Drug Resistance, Binding Analysis, HYDROLASE-HYDROLASE INHIBITOR complex; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier60.07
Radius of gyration Rg (electron density) rg_electron59.59
Forward intensity I(0) i06824410000.00
Molecular weight molecular_weight703360.0 kDa
Excluded volume excluded_volume882380 ų
Envelope volume envelope_volume1254100 ų
Hydration-shell volume shell_volume168430 ų
Envelope diameter envelope_diameter194.2
Shell Rg shell_rg67.83
Envelope Rg envelope_rg57.61
Shape Rg shape_rg59.58
Total Rg total_rg59.82
Total atoms total_atoms49555
Residues n_residues6344
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 dmax189.2
Rg (real space) rg_real59.79
Rg uncertainty (real space) rg_real_error1.74
I(0) (real space) i0_real6.8240e+09
I(0) uncertainty (real space) i0_real_error1.2980e+08
Rg (reciprocal space) rg_reciprocal60.29
I(0) (reciprocal space) i0_reciprocal6830000000.0000
Solution quality estimate total_estimate0.8072
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary80.0
Skewness Skewness skewness0.209
Kurtosis Kurtosis kurtosis-0.414
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha964100000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.843; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (18)

7. Fold Classification (SCOP + CATH) 54 domains

SCOP 2.08 (26 domains)

Domain ID domain_idd4qwua_
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_idd4qwub_
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_idd4qwuc1
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_idd4qwuc2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4qwue_
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_idd4qwuf_
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_idd4qwug_
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_idd4qwuh_
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_idd4qwui_
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_idd4qwuj_
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_idd4qwuk_
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_idd4qwul_
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_idd4qwum_
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_idd4qwun_
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_idd4qwuo_
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_idd4qwup_
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_idd4qwuq1
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_idd4qwuq2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd4qwus_
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_idd4qwut_
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_idd4qwuu_
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_idd4qwuv_
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_idd4qwuw_
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_idd4qwux_
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_idd4qwuy_
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_idd4qwuz_
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 (28 domains)

Domain ID domain_id4qwuA00
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_id4qwuB00
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_id4qwuC00
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_id4qwuD00
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_id4qwuE00
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_id4qwuF00
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_id4qwuG00
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_id4qwuH00
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_id4qwuI00
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_id4qwuJ00
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_id4qwuK00
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_id4qwuL00
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_id4qwuM00
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_id4qwuN00
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_id4qwuO00
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_id4qwuP00
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_id4qwuQ00
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_id4qwuR00
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_id4qwuS00
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_id4qwuT00
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_id4qwuU00
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_id4qwuV00
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_id4qwuW00
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_id4qwuX00
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_id4qwuY00
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_id4qwuZ00
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_id4qwua00
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_id4qwub00
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)