3gpw

Crystal structure of the yeast 20S proteasome in complex with Salinosporamide derivatives: irreversible inhibitor ligand

Method: X-RAY DIFFRACTION Dmax: 196.4 Å Quality: GOOD

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

Proteasome component Y7

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 component Y13 × 2 (P23638) Proteasome component PRE6 × 2 (P40303) Proteasome component PUP2 × 2 (P32379) Proteasome component PRE5 × 2 (P40302) Proteasome component C1 × 2 (P21242) Proteasome component C7-alpha × 2 (P21243) Proteasome component PUP1 × 2 (P25043) Proteasome component PUP3 × 2 (P25451) Proteasome component C11 × 2 (P22141) Proteasome component PRE2 × 2 (P30656) Proteasome component C5 × 2 (P23724) Proteasome component PRE4 × 2 (P30657) Proteasome component PRE3 × 2 (P38624) SA1 (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;12% MPD, 0.1M MES, 20mM MgAc2, pH 6.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.50 Å R-free 0.255

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 component Y13

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 2–245 Chain P; UniProt 2–245 Fragment:sequence database residues 2-245 Proteasome component Y7 × 2 (P23639) Proteasome component PRE6 × 2 (P40303) Proteasome component PUP2 × 2 (P32379) Proteasome component PRE5 × 2 (P40302) Proteasome component C1 × 2 (P21242) Proteasome component C7-alpha × 2 (P21243) Proteasome component PUP1 × 2 (P25043) Proteasome component PUP3 × 2 (P25451) Proteasome component C11 × 2 (P22141) Proteasome component PRE2 × 2 (P30656) Proteasome component C5 × 2 (P23724) Proteasome component PRE4 × 2 (P30657) Proteasome component PRE3 × 2 (P38624) SA1 (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;12% MPD, 0.1M MES, 20mM MgAc2, pH 6.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.50 Å R-free 0.255

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 PSA4_YEAST
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–244; UniProt 2–245 Author chain P; PDBConstruct 1–244; UniProt 2–245

Proteasome component PRE6

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 3–243 Chain Q; UniProt 3–243 Fragment:sequence database residues 3-243 Proteasome component Y7 × 2 (P23639) Proteasome component Y13 × 2 (P23638) Proteasome component PUP2 × 2 (P32379) Proteasome component PRE5 × 2 (P40302) Proteasome component C1 × 2 (P21242) Proteasome component C7-alpha × 2 (P21243) Proteasome component PUP1 × 2 (P25043) Proteasome component PUP3 × 2 (P25451) Proteasome component C11 × 2 (P22141) Proteasome component PRE2 × 2 (P30656) Proteasome component C5 × 2 (P23724) Proteasome component PRE4 × 2 (P30657) Proteasome component PRE3 × 2 (P38624) SA1 (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;12% MPD, 0.1M MES, 20mM MgAc2, pH 6.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.50 Å R-free 0.255

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 PSA7_YEAST
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–241; UniProt 3–243 Author chain Q; PDBConstruct 1–241; UniProt 3–243

Proteasome component PUP2

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 9–250 Chain R; UniProt 9–250 Fragment:sequence database residues 9-250 Proteasome component Y7 × 2 (P23639) Proteasome component Y13 × 2 (P23638) Proteasome component PRE6 × 2 (P40303) Proteasome component PRE5 × 2 (P40302) Proteasome component C1 × 2 (P21242) Proteasome component C7-alpha × 2 (P21243) Proteasome component PUP1 × 2 (P25043) Proteasome component PUP3 × 2 (P25451) Proteasome component C11 × 2 (P22141) Proteasome component PRE2 × 2 (P30656) Proteasome component C5 × 2 (P23724) Proteasome component PRE4 × 2 (P30657) Proteasome component PRE3 × 2 (P38624) SA1 (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;12% MPD, 0.1M MES, 20mM MgAc2, pH 6.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.50 Å R-free 0.255

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 1–242; UniProt 9–250 Author chain R; PDBConstruct 1–242; UniProt 9–250

Proteasome component PRE5

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 2–234 Chain S; UniProt 2–234 Fragment:sequence database residues 2-234 Proteasome component Y7 × 2 (P23639) Proteasome component Y13 × 2 (P23638) Proteasome component PRE6 × 2 (P40303) Proteasome component PUP2 × 2 (P32379) Proteasome component C1 × 2 (P21242) Proteasome component C7-alpha × 2 (P21243) Proteasome component PUP1 × 2 (P25043) Proteasome component PUP3 × 2 (P25451) Proteasome component C11 × 2 (P22141) Proteasome component PRE2 × 2 (P30656) Proteasome component C5 × 2 (P23724) Proteasome component PRE4 × 2 (P30657) Proteasome component PRE3 × 2 (P38624) SA1 (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;12% MPD, 0.1M MES, 20mM MgAc2, pH 6.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.50 Å R-free 0.255

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 PSA1_YEAST
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–233; UniProt 2–234 Author chain S; PDBConstruct 1–233; UniProt 2–234

Proteasome component C1

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 5–248 Chain T; UniProt 5–248 Fragment:sequence database residues 5-248 Proteasome component Y7 × 2 (P23639) Proteasome component Y13 × 2 (P23638) Proteasome component PRE6 × 2 (P40303) Proteasome component PUP2 × 2 (P32379) Proteasome component PRE5 × 2 (P40302) Proteasome component C7-alpha × 2 (P21243) Proteasome component PUP1 × 2 (P25043) Proteasome component PUP3 × 2 (P25451) Proteasome component C11 × 2 (P22141) Proteasome component PRE2 × 2 (P30656) Proteasome component C5 × 2 (P23724) Proteasome component PRE4 × 2 (P30657) Proteasome component PRE3 × 2 (P38624) SA1 (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;12% MPD, 0.1M MES, 20mM MgAc2, pH 6.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.50 Å R-free 0.255

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 PSA3_YEAST
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–244; UniProt 5–248 Author chain T; PDBConstruct 1–244; UniProt 5–248

Proteasome component C7-alpha

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 10–252 Chain U; UniProt 10–252 Fragment:sequence database residues 10-252 Proteasome component Y7 × 2 (P23639) Proteasome component Y13 × 2 (P23638) Proteasome component PRE6 × 2 (P40303) Proteasome component PUP2 × 2 (P32379) Proteasome component PRE5 × 2 (P40302) Proteasome component C1 × 2 (P21242) Proteasome component PUP1 × 2 (P25043) Proteasome component PUP3 × 2 (P25451) Proteasome component C11 × 2 (P22141) Proteasome component PRE2 × 2 (P30656) Proteasome component C5 × 2 (P23724) Proteasome component PRE4 × 2 (P30657) Proteasome component PRE3 × 2 (P38624) SA1 (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;12% MPD, 0.1M MES, 20mM MgAc2, pH 6.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.50 Å R-free 0.255

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 PSA6_YEAST
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–243; UniProt 10–252 Author chain U; PDBConstruct 1–243; UniProt 10–252

Proteasome component PUP1

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 30–251 Chain V; UniProt 30–251 Fragment:sequence database residues 30-251 Proteasome component Y7 × 2 (P23639) Proteasome component Y13 × 2 (P23638) Proteasome component PRE6 × 2 (P40303) Proteasome component PUP2 × 2 (P32379) Proteasome component PRE5 × 2 (P40302) Proteasome component C1 × 2 (P21242) Proteasome component C7-alpha × 2 (P21243) Proteasome component PUP3 × 2 (P25451) Proteasome component C11 × 2 (P22141) Proteasome component PRE2 × 2 (P30656) Proteasome component C5 × 2 (P23724) Proteasome component PRE4 × 2 (P30657) Proteasome component PRE3 × 2 (P38624) SA1 (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;12% MPD, 0.1M MES, 20mM MgAc2, pH 6.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.50 Å R-free 0.255

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 8
Chains and sequence ranges Author chain H; PDBConstruct 1–222; UniProt 30–251 Author chain V; PDBConstruct 1–222; UniProt 30–251

Proteasome component PUP3

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 2–205 Chain W; UniProt 2–205 Fragment:sequence database residues 2-205 Proteasome component Y7 × 2 (P23639) Proteasome component Y13 × 2 (P23638) Proteasome component PRE6 × 2 (P40303) Proteasome component PUP2 × 2 (P32379) Proteasome component PRE5 × 2 (P40302) Proteasome component C1 × 2 (P21242) Proteasome component C7-alpha × 2 (P21243) Proteasome component PUP1 × 2 (P25043) Proteasome component C11 × 2 (P22141) Proteasome component PRE2 × 2 (P30656) Proteasome component C5 × 2 (P23724) Proteasome component PRE4 × 2 (P30657) Proteasome component PRE3 × 2 (P38624) SA1 (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;12% MPD, 0.1M MES, 20mM MgAc2, pH 6.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.50 Å R-free 0.255

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 1–204; UniProt 2–205 Author chain W; PDBConstruct 1–204; UniProt 2–205

Proteasome component C11

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 Fragment:sequence database residues 1-198 Proteasome component Y7 × 2 (P23639) Proteasome component Y13 × 2 (P23638) Proteasome component PRE6 × 2 (P40303) Proteasome component PUP2 × 2 (P32379) Proteasome component PRE5 × 2 (P40302) Proteasome component C1 × 2 (P21242) Proteasome component C7-alpha × 2 (P21243) Proteasome component PUP1 × 2 (P25043) Proteasome component PUP3 × 2 (P25451) Proteasome component PRE2 × 2 (P30656) Proteasome component C5 × 2 (P23724) Proteasome component PRE4 × 2 (P30657) Proteasome component PRE3 × 2 (P38624) SA1 (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;12% MPD, 0.1M MES, 20mM MgAc2, pH 6.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.50 Å R-free 0.255

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 PSB2_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 component PRE2

OrganismNot specified

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 Fragment:sequence database residues 76-287 Proteasome component Y7 × 2 (P23639) Proteasome component Y13 × 2 (P23638) Proteasome component PRE6 × 2 (P40303) Proteasome component PUP2 × 2 (P32379) Proteasome component PRE5 × 2 (P40302) Proteasome component C1 × 2 (P21242) Proteasome component C7-alpha × 2 (P21243) Proteasome component PUP1 × 2 (P25043) Proteasome component PUP3 × 2 (P25451) Proteasome component C11 × 2 (P22141) Proteasome component C5 × 2 (P23724) Proteasome component PRE4 × 2 (P30657) Proteasome component PRE3 × 2 (P38624) SA1 (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;12% MPD, 0.1M MES, 20mM MgAc2, pH 6.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.50 Å R-free 0.255

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 component C5

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 Fragment:sequence database residues 20-241 Proteasome component Y7 × 2 (P23639) Proteasome component Y13 × 2 (P23638) Proteasome component PRE6 × 2 (P40303) Proteasome component PUP2 × 2 (P32379) Proteasome component PRE5 × 2 (P40302) Proteasome component C1 × 2 (P21242) Proteasome component C7-alpha × 2 (P21243) Proteasome component PUP1 × 2 (P25043) Proteasome component PUP3 × 2 (P25451) Proteasome component C11 × 2 (P22141) Proteasome component PRE2 × 2 (P30656) Proteasome component PRE4 × 2 (P30657) Proteasome component PRE3 × 2 (P38624) SA1 (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;12% MPD, 0.1M MES, 20mM MgAc2, pH 6.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.50 Å R-free 0.255

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 PSB1_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 component PRE4

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 1; UniProt 34–266 Chain M; UniProt 34–266 Fragment:sequence database residues 34-266 Proteasome component Y7 × 2 (P23639) Proteasome component Y13 × 2 (P23638) Proteasome component PRE6 × 2 (P40303) Proteasome component PUP2 × 2 (P32379) Proteasome component PRE5 × 2 (P40302) Proteasome component C1 × 2 (P21242) Proteasome component C7-alpha × 2 (P21243) Proteasome component PUP1 × 2 (P25043) Proteasome component PUP3 × 2 (P25451) Proteasome component C11 × 2 (P22141) Proteasome component PRE2 × 2 (P30656) Proteasome component C5 × 2 (P23724) Proteasome component PRE3 × 2 (P38624) SA1 (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;12% MPD, 0.1M MES, 20mM MgAc2, pH 6.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.50 Å R-free 0.255

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 PSB4_YEAST
Isoform
PDB entities 13
Chains and sequence ranges Author chain 1; PDBConstruct 1–233; UniProt 34–266 Author chain M; PDBConstruct 1–233; UniProt 34–266

Proteasome component PRE3

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 2; UniProt 20–215 Chain N; UniProt 20–215 Fragment:sequence database residues 20-215 Proteasome component Y7 × 2 (P23639) Proteasome component Y13 × 2 (P23638) Proteasome component PRE6 × 2 (P40303) Proteasome component PUP2 × 2 (P32379) Proteasome component PRE5 × 2 (P40302) Proteasome component C1 × 2 (P21242) Proteasome component C7-alpha × 2 (P21243) Proteasome component PUP1 × 2 (P25043) Proteasome component PUP3 × 2 (P25451) Proteasome component C11 × 2 (P22141) Proteasome component PRE2 × 2 (P30656) Proteasome component C5 × 2 (P23724) Proteasome component PRE4 × 2 (P30657) SA1 (3AR,6R,6AS)-6-((S)-((S)-CYCLOHEX-2-ENYL)(HYDROXY)METHYL)-6A-METHYL-4-OXO-HEXAHYDRO-2H-FURO[3,2-C]PYRROLE-6-CARBALDEHYDE × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.7;12% MPD, 0.1M MES, 20mM MgAc2, pH 6.7, VAPOR DIFFUSION, HANGING DROP Resolution 2.50 Å R-free 0.255

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 PSB6_YEAST
Isoform
PDB entities 14
Chains and sequence ranges Author chain 2; PDBConstruct 1–196; UniProt 20–215 Author chain N; 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 3gpw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3gpw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3gpw
Deposition date deposition_date2009-03-23
Structure title titleCrystal structure of the yeast 20S proteasome in complex with Salinosporamide derivatives: irreversible inhibitor ligand
Keywords keywords;proteasome, ubiquitin, cancer therapy, immunology, time-dependent elimination of a defined leaving group, Cytoplasm, Hydrolase, Nucleus, Phosphoprotein, Protease, Threonine protease, Isopeptide bond, Ubl conjugation, Zymogen ;; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier60.44
Radius of gyration Rg (electron density) rg_electron59.95
Forward intensity I(0) i06872530000.00
Molecular weight molecular_weight704950.0 kDa
Excluded volume excluded_volume884100 ų
Envelope volume envelope_volume1259200 ų
Hydration-shell volume shell_volume168730 ų
Envelope diameter envelope_diameter197.8
Shell Rg shell_rg67.89
Envelope Rg envelope_rg57.80
Shape Rg shape_rg59.93
Total Rg total_rg60.17
Total atoms total_atoms49668
Residues n_residues6164
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 dmax196.4
Rg (real space) rg_real60.15
Rg uncertainty (real space) rg_real_error1.36
I(0) (real space) i0_real6.8730e+09
I(0) uncertainty (real space) i0_real_error1.2680e+08
Rg (reciprocal space) rg_reciprocal60.65
I(0) (reciprocal space) i0_reciprocal6878000000.0000
Solution quality estimate total_estimate0.8559
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary75.5
Skewness Skewness skewness0.210
Kurtosis Kurtosis kurtosis-0.415
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1099000000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.791; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.955; Smooth: 0.793

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

7. Fold Classification (SCOP + CATH) 56 domains

SCOP 2.08 (28 domains)

Domain ID domain_idd3gpw1_
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_idd3gpw2_
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_idd3gpwa_
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_idd3gpwb_
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_idd3gpwc_
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_idd3gpwd_
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_idd3gpwe_
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_idd3gpwf_
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_idd3gpwg_
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_idd3gpwh_
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_idd3gpwi_
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_idd3gpwj_
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_idd3gpwk_
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_idd3gpwl_
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_idd3gpwm_
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_idd3gpwn_
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_idd3gpwo_
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_idd3gpwp_
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_idd3gpwq_
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_idd3gpwr_
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_idd3gpws_
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_idd3gpwt_
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_idd3gpwu_
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_idd3gpwv_
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_idd3gpww_
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_idd3gpwx_
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_idd3gpwy_
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_idd3gpwz_
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_id3gpw100
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_id3gpw200
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_id3gpwA00
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_id3gpwB00
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_id3gpwC00
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_id3gpwD00
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_id3gpwE00
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_id3gpwF00
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_id3gpwG00
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_id3gpwH00
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_id3gpwI00
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_id3gpwJ00
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_id3gpwK00
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_id3gpwL00
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_id3gpwM00
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_id3gpwN00
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_id3gpwO00
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_id3gpwP00
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_id3gpwQ00
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_id3gpwR00
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_id3gpwS00
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_id3gpwT00
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_id3gpwU00
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_id3gpwV00
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_id3gpwW00
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_id3gpwX00
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_id3gpwY00
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_id3gpwZ00
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)