4qwr

yCP beta5-C52F mutant in complex with carfilzomib

Method: X-RAY DIFFRACTION

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

Proteasome subunit alpha type-2

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 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） MAGNESIUM ION × 8 CHLORIDE ION × 4 ;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 ; × 6 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 28	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 subunit alpha type-3

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 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） MAGNESIUM ION × 8 CHLORIDE ION × 4 ;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 ; × 6 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 28	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	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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 8 CHLORIDE ION × 4 ;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 ; × 6 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 28	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	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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 8 CHLORIDE ION × 4 ;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 ; × 6 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 28	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 subunit alpha type-6

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 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） MAGNESIUM ION × 8 CHLORIDE ION × 4 ;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 ; × 6 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 28	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	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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 8 CHLORIDE ION × 4 ;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 ; × 6 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 28	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	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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 8 CHLORIDE ION × 4 ;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 ; × 6 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 28	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	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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 8 CHLORIDE ION × 4 ;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 ; × 6 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 28	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	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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 8 CHLORIDE ION × 4 ;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 ; × 6 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 28	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 1–205； 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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 8 CHLORIDE ION × 4 ;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 ; × 6 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 28	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	10
Chains and sequence ranges	Author chain J； PDBConstruct 1–198； UniProt 1–198 Author chain X； PDBConstruct 1–198； UniProt 1–198

Proteasome subunit beta type-5

Saccharomyces cerevisiae

UniProt P30656

State in the Current Structure

Assembly	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 8 CHLORIDE ION × 4 ;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 ; × 6 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 28	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 subunit beta type-6

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 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） MAGNESIUM ION × 8 CHLORIDE ION × 4 ;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 ; × 6 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 28	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	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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 8 CHLORIDE ION × 4 ;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 ; × 6 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 28	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	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	Physical composition	Protein state	Molecular copy count	Associated components	Data consistency
1	Protein heterocomplex	Heteromer	Protein 28	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） MAGNESIUM ION × 8 CHLORIDE ION × 4 ;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 ; × 6 2-(N-MORPHOLINO)-ETHANESULFONIC ACID × 2 water × 28	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	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.

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	4qwr
Deposition date deposition_date	2014-07-17
Structure title title	yCP beta5-C52F mutant in complex with carfilzomib
Keywords keywords	Cancer, Proteasome, Bortezomib, Drug Resistance, Binding Analysis, HYDROLASE-HYDROLASE INHIBITOR complex; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method method	X-RAY DIFFRACTION

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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.

4qwr__assembly_1__model_1

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

Download this curve (.dat)

4qwr__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

4qwr__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	60.27 Å
Rg (electron density)	59.75 Å
Total Rg	59.97 Å
Atom count	49654
Residues	6336
Excluded volume	884830 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`4qwr__assembly_1__model_1`	28-meric （28）	Success	4.1.3-1-20251215 (887e7ef)	View Download

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4. Crystallography and Experiment 4. Crystallography & Experiment

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5. Entities and Polymers Entities & Polymers (19)

Entity 1 Entity 1 polymer

Description description	Proteasome subunit alpha type-2
Molecular weight formula_weight	27191.8 kDa
EC 编号 ec_number	3.4.25.1
Mutation mutation	C52F
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	49927

MTDRYSFSLTTFSPSGKLGQIDYALTAVKQGVTSLGIKATNGVVIATEKKSSSPLAMSETLSKVSLLTPDIGAVYSGMGPDYRVLVDKSRKVAHTSYKRIYGEYPPTKLLVSEVAKIMQEATQSGGVRPFGVSLLIAGHDEFNGFSLYQVDPSGSYFPWKATAIGKGSVAAKTFLEKRWNDELELEDAIHIALLTLKESVEGEFNGDTIELAIIGDENPDLLGYTGIPTDKGPRFRKLTSQEINDRLEAL

Entity 2 Entity 2 polymer

Description description	Proteasome subunit alpha type-3
Molecular weight formula_weight	28748.2 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	B,P

MGSRRYDSRTTIFSPEGRLYQVEYALESISHAGTAIGIMASDGIVLAAERKVTSTLLEQDTSTEKLYKLNDKIAVAVAGLTADAEILINTARIHAQNYLKTYNEDIPVEILVRRLSDIKQGYTQHGGLRPFGVSFIYAGYDDRYGYQLYTSNPSGNYTGWKAISVGANTSAAQTLLQMDYKDDMKVDDAIELALKTLSKTTDSSALTYDRLEFATIRKGANDGEVYQKIFKPQEIKDILVKTGITKKDEDEEADEDMK

Entity 3 Entity 3 polymer

Description description	Proteasome subunit alpha type-4
Molecular weight formula_weight	28478.1 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	C,Q

MSGYDRALSIFSPDGHIFQVEYALEAVKRGTCAVGVKGKNCVVLGCERRSTLKLQDTRITPSKVSKIDSHVVLSFSGLNADSRILIEKARVEAQSHRLTLEDPVTVEYLTRYVAGVQQRYTQSGGVRPFGVSTLIAGFDPRDDEPKLYQTEPSGIYSSWSAQTIGRNSKTVREFLEKNYDRKEPPATVEECVKLTVRSLLEVVQTGAKNIEITVVKPDSDIVALSSEEINQYVTQIEQEKQEQQEQDKKKKSNH

Entity 4 Entity 4 polymer

Description description	Proteasome subunit alpha type-5
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 subunit alpha type-6
Molecular weight formula_weight	25634.0 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	E,S

MFRNNYDGDTVTFSPTGRLFQVEYALEAIKQGSVTVGLRSNTHAVLVALKRNADELSSYQKKIIKCDEHMGLSLAGLAPDARVLSNYLRQQCNYSSLVFNRKLAVERAGHLLCDKAQKNTQSYGGRPYGVGLLIIGYDKSGAHLLEFQPSGNVTELYGTAIGARSQGAKTYLERTLDTFIKIDGNPDELIKAGVEAISQSLRDESLTVDNLSIAIVGKDTPFTIYDGEAVAKYI

Entity 6 Entity 6 polymer

Description description	Probable proteasome subunit alpha type-7
Molecular weight formula_weight	31575.1 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	F,T

MTSIGTGYDLSNSVFSPDGRNFQVEYAVKAVENGTTSIGIKCNDGVVFAVEKLITSKLLVPQKNVKIQVVDRHIGCVYSGLIPDGRHLVNRGREEAASFKKLYKTPIPIPAFADRLGQYVQAHTLYNSVRPFGVSTIFGGVDKNGAHLYMLEPSGSYWGYKGAATGKGRQSAKAELEKLVDHHPEGLSAREAVKQAAKIIYLAHEDNKEKDFELEISWCSLSETNGLHKFVKGDLLQEAIDFAQKEINGDDDEDEDDSDNVMSSDDENAPVATNANATTDQEGDIHLE

Entity 7 Entity 7 polymer

Description description	Proteasome subunit alpha type-1
Molecular weight formula_weight	28033.8 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	G,U

MSGAAAASAAGYDRHITIFSPEGRLYQVEYAFKATNQTNINSLAVRGKDCTVVISQKKVPDKLLDPTTVSYIFCISRTIGMVVNGPIPDARNAALRAKAEAAEFRYKYGYDMPCDVLAKRMANLSQIYTQRAYMRPLGVILTFVSVDEELGPSIYKTDPAGYYVGYKATATGPKQQEITTNLENHFKKSKIDHINEESWEKVVEFAITHMIDALGTEFSKNDLEVGVATKDKFFTLSAENIEERLVAIAEQD

Entity 8 Entity 8 polymer

Description description	Proteasome subunit beta type-2
Molecular weight formula_weight	25114.5 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	H,V

TTIVGVKFNNGVVIAADTRSTQGPIVADKNCAKLHRISPKIWCAGAGTAADTEAVTQLIGSNIELHSLYTSREPRVVSALQMLKQHLFKYQGHIGAYLIVAGVDPTGSHLFSIHAHGSTDVGYYLSLGSGSLAAMAVLESHWKQDLTKEEAIKLASDAIQAGIWNDLGSGSNVDVCVMEIGKDAEYLRNYLTPNVREEKQKSYKFPRGTTAVLKESIVNICDIQEEQVDITA

Entity 9 Entity 9 polymer

Description description	Proteasome subunit beta type-3
Molecular weight formula_weight	22627.8 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	I,W

MSDPSSINGGIVVAMTGKDCVAIACDLRLGSQSLGVSNKFEKIFHYGHVFLGITGLATDVTTLNEMFRYKTNLYKLKEERAIEPETFTQLVSSSLYERRFGPYFVGPVVAGINSKSGKPFIAGFDLIGCIDEAKDFIVSGTASDQLFGMCESLYEPNLEPEDLFETISQALLNAADRDALSGWGAVVYIIKKDEVVKRYLKMRQD

Entity 10 Entity 10 polymer

Description description	Proteasome subunit beta type-4
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 subunit beta type-5
Molecular weight formula_weight	23369.3 kDa
EC 编号 ec_number	3.4.25.1
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

TTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADFQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG

Source Source

Source organism organism	Saccharomyces cerevisiae
Common name common_name	;Baker's yeast ;
NCBI taxonomy ID ncbi_taxonomy_id	559292
Host organism host_organism	SACCHAROMYCES CEREVISIAE

Entity 12 Entity 12 polymer

Description description	Proteasome subunit beta type-6
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 subunit beta type-7
Molecular weight formula_weight	27200.9 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	M,a

TQIANAGASPMVNTQQPIVTGTSVISMKYDNGVIIAADNLGSYGSLLRFNGVERLIPVGDNTVVGISGDISDMQHIERLLKDLVTENAYDNPLADAEEALEPSYIFEYLATVMYQRRSKMNPLWNAIIVAGVQSNGDQFLRYVNLLGVTYSSPTLATGFGAHMANPLLRKVVDRESDIPKTTVQVAEEAIVNAMRVLYYRDARSSRNFSLAIIDKNTGLTFKKNLQVENMKWDFAKDIKGYGTQKI

Entity 14 Entity 14 polymer

Description description	Proteasome subunit beta type-1
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,b

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	8

Entity 16 Entity 16 non-polymer

Description description	CHLORIDE ION
Molecular weight formula_weight	35.5 kDa
Source method src_method	syn
Copy count entity_count	4

Entity 17 Entity 17 non-polymer

Description description	;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 ;
Molecular weight formula_weight	723.9 kDa
Source method src_method	syn
Copy count entity_count	6

Entity 18 Entity 18 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 19 Entity 19 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	273

▼

6. Fold Classification (SCOP + CATH) 56 domains

SCOP 2.08 (28 domains)

Domain ID domain_id	d4qwra_
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	d4qwrb_
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	d4qwrc1
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.153.1.0 — automated matches

Domain ID domain_id	d4qwrc2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4qwrd_
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	d4qwre_
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	d4qwrf_
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	d4qwrg_
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	d4qwrh_
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	d4qwri_
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	d4qwrj_
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	d4qwrk_
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	d4qwrl_
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	d4qwrm_
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	d4qwrn_
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	d4qwro_
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	d4qwrp_
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	d4qwrq1
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.153.1.0 — automated matches

Domain ID domain_id	d4qwrq2
Class class	l — Artifacts
Fold Fold fold	l.1 — Tags
Superfamily Superfamily superfamily	l.1.1 — Tags
Family Family family	l.1.1.1 — Tags

Domain ID domain_id	d4qwrr_
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	d4qwrs_
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	d4qwrt_
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	d4qwru_
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	d4qwrv_
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	d4qwrw_
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	d4qwrx_
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	d4qwry_
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	d4qwrz_
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	4qwrA00
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	4qwrB00
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	4qwrC00
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	4qwrD00
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	4qwrE00
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	4qwrF00
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	4qwrG00
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	4qwrH00
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	4qwrI00
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	4qwrJ00
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	4qwrK00
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	4qwrL00
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	4qwrM00
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	4qwrN00
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	4qwrO00
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	4qwrP00
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	4qwrQ00
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	4qwrR00
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	4qwrS00
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	4qwrT00
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	4qwrU00
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	4qwrV00
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	4qwrW00
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	4qwrX00
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	4qwrY00
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	4qwrZ00
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	4qwra00
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	4qwrb00
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	136.000 Å
Unit-cell length b length_b	300.580 Å
Unit-cell length c length_c	144.520 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	2.900 Å
Low-resolution limit resolution_low	15.000 Å
R factor r_factor	0.1820
R_work r_work	0.1806
R_free r_free	0.2094

yCP beta5-C52F mutant in complex with carfilzomib

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

Proteasome subunit alpha type-2

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 subunit alpha type-3

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 subunit alpha type-4

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 subunit alpha type-5

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 subunit alpha type-6

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer

Other homooligomers

Heteromeric or nucleic-acid complex

Probable proteasome subunit alpha type-7

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 subunit alpha type-1

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 subunit beta type-2

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 subunit beta type-3

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 subunit beta type-4

State in the Current Structure

Other States of the Same Protein in the Database

Monomer

Homodimer

Homotetramer