3sdi

Structure of yeast 20S open-gate proteasome with Compound 20

Method: X-RAY DIFFRACTION

▼

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

Proteasome component Y7

OrganismNot specified

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 20 ;N~4~-(2,2-dimethylpropyl)-N~1~-{(2S)-1-[(4-methylbenzyl)amino]-1-oxo-4-phenylbutan-2-yl}-N~2~-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-aspartamide ; × 2 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 20 ;N~4~-(2,2-dimethylpropyl)-N~1~-{(2S)-1-[(4-methylbenzyl)amino]-1-oxo-4-phenylbutan-2-yl}-N~2~-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-aspartamide ; × 2 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PSA4_YEAST
Isoform	—
PDB entities	2
Chains and sequence ranges	Author chain B； PDBConstruct 1–235； UniProt 11–245 Author chain P； PDBConstruct 1–235； UniProt 11–245

Proteasome component PRE6

OrganismNot specified

UniProt P40303

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 20 ;N~4~-(2,2-dimethylpropyl)-N~1~-{(2S)-1-[(4-methylbenzyl)amino]-1-oxo-4-phenylbutan-2-yl}-N~2~-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-aspartamide ; × 2 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 20 ;N~4~-(2,2-dimethylpropyl)-N~1~-{(2S)-1-[(4-methylbenzyl)amino]-1-oxo-4-phenylbutan-2-yl}-N~2~-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-aspartamide ; × 2 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

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 component PRE5

OrganismNot specified

UniProt P40302

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 20 ;N~4~-(2,2-dimethylpropyl)-N~1~-{(2S)-1-[(4-methylbenzyl)amino]-1-oxo-4-phenylbutan-2-yl}-N~2~-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-aspartamide ; × 2 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 20 ;N~4~-(2,2-dimethylpropyl)-N~1~-{(2S)-1-[(4-methylbenzyl)amino]-1-oxo-4-phenylbutan-2-yl}-N~2~-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-aspartamide ; × 2 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PSA3_YEAST
Isoform	—
PDB entities	6
Chains and sequence ranges	Author chain F； PDBConstruct 1–242； UniProt 7–248 Author chain T； PDBConstruct 1–242； UniProt 7–248

Proteasome component C7-alpha

OrganismNot specified

UniProt P21243

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 20 ;N~4~-(2,2-dimethylpropyl)-N~1~-{(2S)-1-[(4-methylbenzyl)amino]-1-oxo-4-phenylbutan-2-yl}-N~2~-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-aspartamide ; × 2 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 20 ;N~4~-(2,2-dimethylpropyl)-N~1~-{(2S)-1-[(4-methylbenzyl)amino]-1-oxo-4-phenylbutan-2-yl}-N~2~-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-aspartamide ; × 2 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 20 ;N~4~-(2,2-dimethylpropyl)-N~1~-{(2S)-1-[(4-methylbenzyl)amino]-1-oxo-4-phenylbutan-2-yl}-N~2~-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-aspartamide ; × 2 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 20 ;N~4~-(2,2-dimethylpropyl)-N~1~-{(2S)-1-[(4-methylbenzyl)amino]-1-oxo-4-phenylbutan-2-yl}-N~2~-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-aspartamide ; × 2 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 20 ;N~4~-(2,2-dimethylpropyl)-N~1~-{(2S)-1-[(4-methylbenzyl)amino]-1-oxo-4-phenylbutan-2-yl}-N~2~-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-aspartamide ; × 2 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 20 ;N~4~-(2,2-dimethylpropyl)-N~1~-{(2S)-1-[(4-methylbenzyl)amino]-1-oxo-4-phenylbutan-2-yl}-N~2~-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-aspartamide ; × 2 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 20 ;N~4~-(2,2-dimethylpropyl)-N~1~-{(2S)-1-[(4-methylbenzyl)amino]-1-oxo-4-phenylbutan-2-yl}-N~2~-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-aspartamide ; × 2 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

View Construct and Data Evidence

UniProt name	PSB4_YEAST
Isoform	—
PDB entities	13
Chains and sequence ranges	Author chain 1； PDBConstruct 1–220； UniProt 34–266 Author chain M； PDBConstruct 1–220； UniProt 34–266

Proteasome component PRE3

OrganismNot specified

UniProt P38624

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 20 ;N~4~-(2,2-dimethylpropyl)-N~1~-{(2S)-1-[(4-methylbenzyl)amino]-1-oxo-4-phenylbutan-2-yl}-N~2~-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-aspartamide ; × 2 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 1	Consistent with protein count

Other States of the Same Protein in the Database

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.

▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id	3sdi
Deposition date deposition_date	2011-06-09
Structure title title	Structure of yeast 20S open-gate proteasome with Compound 20
Keywords keywords	20S proteasome, Hydrolase-Hydrolase Inhibitor complex; Hydrolase/Hydrolase Inhibitor
Experimental Method method	X-RAY DIFFRACTION

▼

3. Official assembly/model SAXS Official SAXS Profiles

This page reads only the latest assembly calculations. Every curve maps to an explicit PDB entry, official biological assembly and coordinate model.

3sdi__assembly_1__model_1

Assembly 1 · Model 1 · CRYSOL 4.1.3-1-20251215 (887e7ef)

Download this curve (.dat)

3sdi__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

3sdi__assembly_1__model_1 | P(r) · Pending

P(r) will be calculated and displayed separately for the same assembly/model.

Rg（Guinier）	60.26 Å
Rg (electron density)	59.79 Å
Total Rg	60.01 Å
Atom count	49011
Residues	6293
Excluded volume	872900 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`3sdi__assembly_1__model_1`	28-meric （28）	Success	4.1.3-1-20251215 (887e7ef)	View Download

▶

4. Crystallography and Experiment 4. Crystallography & Experiment

▶

5. Entities and Polymers Entities & Polymers (18)

Entity 1 Entity 1 polymer

Description description	Proteasome component Y7
Molecular weight formula_weight	27191.8 kDa
EC 编号 ec_number	3.4.25.1
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A,O
Atom count atom_count	49012

MTDRYSFSLTTFSPSGKLGQIDYALTAVKQGVTSLGIKATNGVVIATEKKSSSPLAMSETLSKVSLLTPDIGAVYSGMGPDYRVLVDKSRKVAHTSYKRIYGEYPPTKLLVSEVAKIMQEATQSGGVRPFGVSLLIAGHDEFNGFSLYQVDPSGSYFPWKATAIGKGSVAAKTFLEKRWNDELELEDAIHIALLTLKESVEGEFNGDTIELAIIGDENPDLLGYTGIPTDKGPRFRKLTSQEINDRLEAL

Entity 2 Entity 2 polymer

Description description	Proteasome component Y13
Molecular weight formula_weight	25968.3 kDa
EC 编号 ec_number	3.4.25.1
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	B,P

TIFSPEGRLYQVEYALESISHAGTAIGIMASDGIVLAAERKVTSTLLEQDTSTEKLYKLNDKIAVAVAGLTADAEILINTARIHAQNYLKTYNEDIPVEILVRRLSDIKQGYTQHGGLRPFGVSFIYAGYDDRYGYQLYTSNPSGNYTGWKAISVGANTSAAQTLLQMDYKDDMKVDDAIELALKTLSKTTDSSALTYDRLEFATIRKGANDGEVYQKIFKPQEIKDILVKTGIT

Entity 3 Entity 3 polymer

Description description	Proteasome component PRE6
Molecular weight formula_weight	26903.3 kDa
EC 编号 ec_number	3.4.25.1
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	C,Q

GYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYDRKEPPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEKQEQ

Entity 4 Entity 4 polymer

Description description	Proteasome component PUP2
Molecular weight formula_weight	28649.1 kDa
EC 编号 ec_number	3.4.25.1
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	D,R

MFLTRSEYDRGVSTFSPEGRLFQVEYSLEAIKLGSTAIGIATKEGVVLGVEKRATSPLLESDSIEKIVEIDRHIGCAMSGLTADARSMIEHARTAAVTHNLYYDEDINVESLTQSVCDLALRFGEGASGEERLMSRPFGVALLIAGHDADDGYQLFHAEPSGTFYRYNAKAIGSGSEGAQAELLNEWHSSLTLKEAELLVLKILKQVMEEKLDENNAQLSCITKQDGFKIYDNEKTAELIKELKEKEAAESPEEADVEMS

Entity 5 Entity 5 polymer

Description description	Proteasome component PRE5
Molecular weight formula_weight	25410.7 kDa
EC 编号 ec_number	3.4.25.1
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	E,S

FRNNYDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQKKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSAGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARSQGAKTYLERTLDTFIKIDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDTPFTIYDGEAVAKYI

Entity 6 Entity 6 polymer

Description description	Proteasome component C1
Molecular weight formula_weight	26734.3 kDa
EC 编号 ec_number	3.4.25.1
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	F,T

GYDLSNSVFSPDGRNFQVEYAVKAVENGTTSIGIKCNDGVVFAVEKLITSKLLVPQKNVKIQVVDRHIGCVYSGLIPDGRHLVNRGREEAASFKKLYKTPIPIPAFADRLGQYVQAHTLYNSVRPFGVSTIFGGVDKNGAHLYMLEPSGSYWGYKGAATGKGRQSAKAELEKLVDHHPEGLSAREAVKQAAKIIYLAHEDNKEKDFELEISWCSLSETNGLHKFVKGDLLQEAIDFAQKEIN

Entity 7 Entity 7 polymer

Description description	Proteasome component C7-alpha
Molecular weight formula_weight	27316.0 kDa
EC 编号 ec_number	3.4.25.1
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	G,U

AGYDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATATGPKQQEITTNLENHFKKSKIDHINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKDKFFTLSAENIEERLVAIAEQD

Entity 8 Entity 8 polymer

Description description	Proteasome component PUP1
Molecular weight formula_weight	23987.3 kDa
EC 编号 ec_number	3.4.25.1
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	H,V

TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSALQMLKQHLFKYQGHIGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASDAIQAGIWNDLGSGSNVDVCVMEIGKDAEYLRNYLTPNVREEKQKSYKFPRGTTAVLKESIVNICD

Entity 9 Entity 9 polymer

Description description	Proteasome component PUP3
Molecular weight formula_weight	22496.6 kDa
EC 编号 ec_number	3.4.25.1
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	I,W

SDPSSINGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYGHVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPETFTQLVSSSLYERRFGPYFVGPVVAGINSKSGKPFIAGFDLIGCIDEAKDFIVSGTASDQLFGMCESLYEPNLEPEDLFETISQALLNAADRDALSGWGAVVYIIKKDEVVKRYLKMRQD

Entity 10 Entity 10 polymer

Description description	Proteasome component C11
Molecular weight formula_weight	22545.7 kDa
EC 编号 ec_number	3.4.25.1
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	J,X

MDIILGIRVQDSVILASSKAVTRGISVLKDSDDKTRQLSPHTLMSFAGEAGDTVQFAEYIQANIQLYSIREDYELSPQAVSSFVRQELAKSIRSRRPYQVNVLIGGYDKKKNKPELYQIDYLGTKVELPYGAHGYSGFYTFSLLDHHYRPDMTTEEGLDLLKLCVQELEKRMPMDFKGVIVKIVDKDGIRQVDDFQAQ

Entity 11 Entity 11 polymer

Description description	Proteasome component PRE2
Molecular weight formula_weight	23325.2 kDa
EC 编号 ec_number	3.4.25.1
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	K,Y

TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG

Entity 12 Entity 12 polymer

Description description	Proteasome component C5
Molecular weight formula_weight	24883.9 kDa
EC 编号 ec_number	3.4.25.1
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	L,Z

QFNPYGDNGGTILGIAGEDFAVLAGDTRNITDYSINSRYEPKVFDCGDNIVMSANGFAADGDALVKRFKNSVKWYHFDHNDKKLSINSAARNIQHLLYGKRFFPYYVHTIIAGLDEDGKGAVYSFDPVGSYEREQCRAGGAAASLIMPFLDNQVNFKNQYEPGTNGKVKKPLKYLSVEEVIKLVRDSFTSATERHIQVGDGLEILIVTKDGVRKEFYELKRD

Entity 13 Entity 13 polymer

Description description	Proteasome component PRE4
Molecular weight formula_weight	25945.5 kDa
EC 编号 ec_number	3.4.25.1
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	M,1

TQQPIVTGTSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLLKDLVTENAYDNPLADAEEALEPSYIFEYLATVMYQRRSKMNPLWNAIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFGAHMANPLLRKVVDRESDIPKTTVQVAEEAIVNAMRVLYYRDARSSRNFSLAIIDKNTGLTFKKNLQVENMKWDFAKDIKGYGTQKI

Entity 14 Entity 14 polymer

Description description	Proteasome component PRE3
Molecular weight formula_weight	21517.2 kDa
EC 编号 ec_number	3.4.25.1
Source method src_method	nat
Copy count entity_count	2

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	N,2

TSIMAVTFKDGVILGADSRTTTGAYIANRVTDKLTRVHDKIWCCRSGSAADTQAIADIVQYHLELYTSQYGTPSTETAASVFKELCYENKDNLTAGIIVAGYDDKNKGEVYTIPLGGSVHKLPYAIAGSGSTFIYGYCDKNFRENMSKEETVDFIKHSLSQAIKWDGSSGGVIRMVVLTAAGVERLIFYPDEYEQL

Entity 15 Entity 15 non-polymer

Description description	MAGNESIUM ION
Molecular weight formula_weight	24.3 kDa
Source method src_method	syn
Copy count entity_count	20

Entity 16 Entity 16 non-polymer

Description description	;N~4~-(2,2-dimethylpropyl)-N~1~-{(2S)-1-[(4-methylbenzyl)amino]-1-oxo-4-phenylbutan-2-yl}-N~2~-[(5-methyl-1,2-oxazol-3-yl)carbonyl]-L-aspartamide ;
Molecular weight formula_weight	575.7 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 17 Entity 17 non-polymer

Description description	2-(N-MORPHOLINO)-ETHANESULFONIC ACID
Molecular weight formula_weight	195.2 kDa
Source method src_method	syn
Copy count entity_count	2

Entity 18 Entity 18 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	1

▼

6. Fold Classification (SCOP + CATH) 56 domains

SCOP 2.08 (28 domains)

Domain ID domain_id	d3sdi1_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdi2_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdia_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdib_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdic_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdid_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdie_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdif_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdig_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdih_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdii_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdij_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdik_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdil_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdim_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdin_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdio_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdip_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdiq_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdir_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdis_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdit_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdiu_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdiv_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdiw_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdix_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdiy_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

Domain ID domain_id	d3sdiz_
Class class	d — Alpha and beta proteins (a+b)
Fold Fold fold	d.153 — Ntn hydrolase-like
Superfamily Superfamily superfamily	d.153.1 — N-terminal nucleophile aminohydrolases (Ntn hydrolases)
Family Family family	d.153.1.4 — Proteasome subunits

CATH v4.4 (28 domains)

Domain ID domain_id	3sdi100
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdi200
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiA00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiB00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiC00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiD00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiE00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiF00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiG00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiH00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiI00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiJ00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiK00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiL00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiM00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiN00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiO00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiP00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiQ00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiR00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiS00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiT00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiU00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiV00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiW00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiX00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiY00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

Domain ID domain_id	3sdiZ00
Class class	3 — Alpha Beta
Architecture architecture	60 — 4-Layer Sandwich
Topology topology	20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily	10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

▶

Unit-cell length a length_a	136.600 Å
Unit-cell length b length_b	299.450 Å
Unit-cell length c length_c	145.483 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	113.17 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 1 21 1
Space-group number int_tables_number	4
Crystal system crystal_system	—

Resolution resolution	2.650 Å
Low-resolution limit resolution_low	30.000 Å
R factor r_factor	0.2193
R_work r_work	0.2186
R_free r_free	0.2532

Structure of yeast 20S open-gate proteasome with Compound 20

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

Proteasome component Y7

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Proteasome component Y13

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Proteasome component PRE6

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Proteasome component PUP2

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Proteasome component PRE5

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Proteasome component C1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Proteasome component C7-alpha

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Proteasome component PUP1

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Proteasome component PUP3

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Proteasome component C11

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer