5d0v

Yeast 20S proteasome beta5-T1C mutant in complex with Carfilzomib

Method: X-RAY DIFFRACTION Dmax: 192.3 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 Not recorded 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 × 8 CL CHLORIDE ION × 4 3BV N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 2.90 Å R-free 0.220

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 × 8 CL CHLORIDE ION × 4 3BV N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 2.90 Å R-free 0.220

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 × 8 CL CHLORIDE ION × 4 3BV N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 2.90 Å R-free 0.220

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 × 8 CL CHLORIDE ION × 4 3BV N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 2.90 Å R-free 0.220

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 × 8 CL CHLORIDE ION × 4 3BV N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 2.90 Å R-free 0.220

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 × 8 CL CHLORIDE ION × 4 3BV N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 2.90 Å R-free 0.220

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 × 8 CL CHLORIDE ION × 4 3BV N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 2.90 Å R-free 0.220

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 × 8 CL CHLORIDE ION × 4 3BV N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 2.90 Å R-free 0.220

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 × 8 CL CHLORIDE ION × 4 3BV N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 2.90 Å R-free 0.220

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 × 8 CL CHLORIDE ION × 4 3BV N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 2.90 Å R-free 0.220

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 (strain ATCC 204508 / S288c)

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 70–287 Chain Y; UniProt 70–287 Mutation:T1C 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 × 8 CL CHLORIDE ION × 4 3BV N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 2.90 Å R-free 0.220

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 1–218; UniProt 70–287 Author chain Y; PDBConstruct 1–218; UniProt 70–287

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 × 8 CL CHLORIDE ION × 4 3BV N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 2.90 Å R-free 0.220

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 × 8 CL CHLORIDE ION × 4 3BV N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 2.90 Å R-free 0.220

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 × 8 CL CHLORIDE ION × 4 3BV N-{(2S)-2-[(morpholin-4-ylacetyl)amino]-4-phenylbutanoyl}-L-leucyl-N-[(2R,3S,4S)-1,3-dihydroxy-2,6-dimethylheptan-4-yl]-L-phenylalaninamide × 4 MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.8;293 K;20 mM MgAC2, 13% MPD, 0.1 M MES Resolution 2.90 Å R-free 0.220

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 5d0v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5d0v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5d0v
Deposition date deposition_date2015-08-03
Structure title titleYeast 20S proteasome beta5-T1C mutant in complex with Carfilzomib
Keywords keywordsHYDROLASE-HYDROLASE INHIBITOR complex, Proteasome, Mutant, Inhibitor, Binding Analysis; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier60.16
Radius of gyration Rg (electron density) rg_electron59.67
Forward intensity I(0) i06825510000.00
Molecular weight molecular_weight703900.0 kDa
Excluded volume excluded_volume883310 ų
Envelope volume envelope_volume1259200 ų
Hydration-shell volume shell_volume168880 ų
Envelope diameter envelope_diameter194.3
Shell Rg shell_rg67.91
Envelope Rg envelope_rg57.70
Shape Rg shape_rg59.66
Total Rg total_rg59.88
Total atoms total_atoms49581
Residues n_residues6342
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 dmax192.3
Rg (real space) rg_real59.88
Rg uncertainty (real space) rg_real_error1.54
I(0) (real space) i0_real6.8260e+09
I(0) uncertainty (real space) i0_real_error1.3130e+08
Rg (reciprocal space) rg_reciprocal60.38
I(0) (reciprocal space) i0_reciprocal6831000000.0000
Solution quality estimate total_estimate0.8498
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary74.0
Skewness Skewness skewness0.211
Kurtosis Kurtosis kurtosis-0.408
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1013000000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.817; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.635

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (19)

7. Fold Classification (SCOP + CATH) 56 domains

SCOP 2.08 (28 domains)

Domain ID domain_idd5d0va_
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_idd5d0vb_
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_idd5d0vc1
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_idd5d0vc2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5d0vd_
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_idd5d0ve_
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_idd5d0vf_
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_idd5d0vg_
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_idd5d0vh_
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_idd5d0vi_
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_idd5d0vj_
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_idd5d0vk_
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_idd5d0vl_
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_idd5d0vm_
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_idd5d0vn_
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_idd5d0vo_
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_idd5d0vp_
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_idd5d0vq1
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_idd5d0vq2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd5d0vr_
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_idd5d0vs_
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_idd5d0vt_
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_idd5d0vu_
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_idd5d0vv_
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_idd5d0vw_
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_idd5d0vx_
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_idd5d0vy_
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_idd5d0vz_
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_id5d0vA00
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_id5d0vB00
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_id5d0vC00
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_id5d0vD00
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_id5d0vE00
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_id5d0vF00
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_id5d0vG00
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_id5d0vH00
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_id5d0vI00
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_id5d0vJ00
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_id5d0vK00
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_id5d0vL00
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_id5d0vM00
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_id5d0vN00
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_id5d0vO00
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_id5d0vP00
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_id5d0vQ00
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_id5d0vR00
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_id5d0vS00
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_id5d0vT00
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_id5d0vU00
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_id5d0vV00
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_id5d0vW00
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_id5d0vX00
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_id5d0vY00
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_id5d0vZ00
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_id5d0va00
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_id5d0vb00
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)