5d0v

Yeast 20S proteasome beta5-T1C 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 ; × 4 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 ; × 4 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 ; × 4 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 ; × 4 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 ; × 4 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 ; × 4 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 ; × 4 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 ; × 4 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 ; × 4 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 ; × 4 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 (strain ATCC 204508 / S288c)

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 ; × 4 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 1–218； UniProt 70–287 Author chain Y； PDBConstruct 1–218； UniProt 70–287

Proteasome subunit beta type-6

OrganismNot specified

UniProt P23724

State in the Current Structure

Assembly	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 ; × 4 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 ; × 4 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 ; × 4 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	5d0v
Deposition date deposition_date	2015-08-03
Structure title title	Yeast 20S proteasome beta5-T1C mutant in complex with Carfilzomib
Keywords keywords	HYDROLASE-HYDROLASE INHIBITOR complex, Proteasome, Mutant, Inhibitor, Binding Analysis; 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.

5d0v__assembly_1__model_1

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

Download this curve (.dat)

5d0v__assembly_1__model_1 | I(q)

100 plotted points; both axes use logarithmic scales.

5d0v__assembly_1__model_1 | P(r) · Pending

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

Rg（Guinier）	60.16 Å
Rg (electron density)	59.67 Å
Total Rg	59.88 Å
Atom count	49581
Residues	6342
Excluded volume	883310 Å³
Maximum q	0.500 Å⁻¹

Assembly	Model	Structure unit	Oligomeric description	Status	CRYSOL	Actions
1	1	`5d0v__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
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	49848

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	23949.1 kDa
EC 编号 ec_number	3.4.25.1
Mutation mutation	T1C
Source method src_method	man
Copy count entity_count	2

Polymer Polymer

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

IKIAHGCTTLAFRFQGGIIVAVDSRATAGNWVASQTVKKVIEINPFLLGTMAGGAADCQFWETWLGSQCRLHELREKERISVAAASKILSNLVYQYKGAGLSMGTMICGYTRKEGPTIYYVDSDGTRLKGDIFCVGSGQTFAYGVLDSNYKWDLSVEDALYLGKRSILAAAHRDAYSGGSVNLYHVTEDGWIYHGNHDVGELFWKVKEEEGSFNNVIG

Source Source

Source organism organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
NCBI taxonomy ID ncbi_taxonomy_id	559292
Host organism host_organism	Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

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	4

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	267

▼

6. Fold Classification (SCOP + CATH) 56 domains

SCOP 2.08 (28 domains)

Domain ID domain_id	d5d0va_
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	d5d0vb_
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	d5d0vc1
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	d5d0vc2
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	d5d0vd_
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	d5d0ve_
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	d5d0vf_
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	d5d0vg_
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	d5d0vh_
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	d5d0vi_
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	d5d0vj_
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	d5d0vk_
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	d5d0vl_
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	d5d0vm_
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	d5d0vn_
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	d5d0vo_
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	d5d0vp_
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	d5d0vq1
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	d5d0vq2
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	d5d0vr_
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	d5d0vs_
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	d5d0vt_
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	d5d0vu_
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	d5d0vv_
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	d5d0vw_
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	d5d0vx_
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	d5d0vy_
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	d5d0vz_
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	5d0vA00
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	5d0vB00
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	5d0vC00
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	5d0vD00
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	5d0vE00
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	5d0vF00
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	5d0vG00
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	5d0vH00
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	5d0vI00
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	5d0vJ00
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	5d0vK00
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	5d0vL00
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	5d0vM00
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	5d0vN00
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	5d0vO00
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	5d0vP00
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	5d0vQ00
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	5d0vR00
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	5d0vS00
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	5d0vT00
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	5d0vU00
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	5d0vV00
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	5d0vW00
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	5d0vX00
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	5d0vY00
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	5d0vZ00
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	5d0va00
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	5d0vb00
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	135.170 Å
Unit-cell length b length_b	299.940 Å
Unit-cell length c length_c	144.940 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	112.56 °
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	0.1943
R_work r_work	0.1929
R_free r_free	0.2199

Yeast 20S proteasome beta5-T1C 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