9o3f

Plasmodium falciparum 20S proteasome bound to inhibitor 296

Method: ELECTRON MICROSCOPY Dmax: 187.3 Å Quality: GOOD

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

Proteasome endopeptidase complex

OrganismNot specified

UniProt Q8IAR3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain A; UniProt 1–260 Chain O; UniProt 1–260 Not recorded Proteasome endopeptidase complex × 2 (C6KST3) Proteasome subunit alpha type × 2 (Q8IDG3) Proteasome subunit alpha type × 2 (Q8IDG2) Proteasome subunit alpha type × 2 (Q8IBI3) Proteasome endopeptidase complex × 2 (Q8IK90) Proteasome subunit alpha type-3, putative × 2 (O77396) Proteasome subunit beta type-6, putative × 2 (Q8I0U7) Proteasome subunit beta × 2 (Q8I6T3) Proteasome subunit beta × 2 (Q8I261) Proteasome subunit beta × 2 (Q8IKC9) Proteasome subunit beta type × 2 (Q8IJT1) Proteasome subunit beta × 2 Proteasome subunit beta × 2 (A0A5K1K7U1) A1B73 (3S)-1-({[(3S)-piperidin-3-yl]oxy}acetyl)-N-({4-[4-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl}methyl)piperidine-3-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8IAR3_PLAF7
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–260; UniProt 1–260 Author chain O; PDBConstruct 1–260; UniProt 1–260

Proteasome endopeptidase complex

OrganismNot specified

UniProt C6KST3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain B; UniProt 1–235 Chain P; UniProt 1–235 Not recorded Proteasome endopeptidase complex × 2 (Q8IAR3) Proteasome subunit alpha type × 2 (Q8IDG3) Proteasome subunit alpha type × 2 (Q8IDG2) Proteasome subunit alpha type × 2 (Q8IBI3) Proteasome endopeptidase complex × 2 (Q8IK90) Proteasome subunit alpha type-3, putative × 2 (O77396) Proteasome subunit beta type-6, putative × 2 (Q8I0U7) Proteasome subunit beta × 2 (Q8I6T3) Proteasome subunit beta × 2 (Q8I261) Proteasome subunit beta × 2 (Q8IKC9) Proteasome subunit beta type × 2 (Q8IJT1) Proteasome subunit beta × 2 Proteasome subunit beta × 2 (A0A5K1K7U1) A1B73 (3S)-1-({[(3S)-piperidin-3-yl]oxy}acetyl)-N-({4-[4-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl}methyl)piperidine-3-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name C6KST3_PLAF7
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–235; UniProt 1–235 Author chain P; PDBConstruct 1–235; UniProt 1–235

Proteasome subunit alpha type

OrganismNot specified

UniProt Q8IDG3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain C; UniProt 1–242 Chain Q; UniProt 1–242 Not recorded Proteasome endopeptidase complex × 2 (Q8IAR3) Proteasome endopeptidase complex × 2 (C6KST3) Proteasome subunit alpha type × 2 (Q8IDG2) Proteasome subunit alpha type × 2 (Q8IBI3) Proteasome endopeptidase complex × 2 (Q8IK90) Proteasome subunit alpha type-3, putative × 2 (O77396) Proteasome subunit beta type-6, putative × 2 (Q8I0U7) Proteasome subunit beta × 2 (Q8I6T3) Proteasome subunit beta × 2 (Q8I261) Proteasome subunit beta × 2 (Q8IKC9) Proteasome subunit beta type × 2 (Q8IJT1) Proteasome subunit beta × 2 Proteasome subunit beta × 2 (A0A5K1K7U1) A1B73 (3S)-1-({[(3S)-piperidin-3-yl]oxy}acetyl)-N-({4-[4-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl}methyl)piperidine-3-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8IDG3_PLAF7
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–242; UniProt 1–242 Author chain Q; PDBConstruct 1–242; UniProt 1–242

Proteasome subunit alpha type

OrganismNot specified

UniProt Q8IDG2

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain D; UniProt 1–241 Chain R; UniProt 1–241 Not recorded Proteasome endopeptidase complex × 2 (Q8IAR3) Proteasome endopeptidase complex × 2 (C6KST3) Proteasome subunit alpha type × 2 (Q8IDG3) Proteasome subunit alpha type × 2 (Q8IBI3) Proteasome endopeptidase complex × 2 (Q8IK90) Proteasome subunit alpha type-3, putative × 2 (O77396) Proteasome subunit beta type-6, putative × 2 (Q8I0U7) Proteasome subunit beta × 2 (Q8I6T3) Proteasome subunit beta × 2 (Q8I261) Proteasome subunit beta × 2 (Q8IKC9) Proteasome subunit beta type × 2 (Q8IJT1) Proteasome subunit beta × 2 Proteasome subunit beta × 2 (A0A5K1K7U1) A1B73 (3S)-1-({[(3S)-piperidin-3-yl]oxy}acetyl)-N-({4-[4-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl}methyl)piperidine-3-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8IDG2_PLAF7
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–241; UniProt 1–241 Author chain R; PDBConstruct 1–241; UniProt 1–241

Proteasome subunit alpha type

OrganismNot specified

UniProt Q8IBI3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain E; UniProt 1–256 Chain S; UniProt 1–256 Not recorded Proteasome endopeptidase complex × 2 (Q8IAR3) Proteasome endopeptidase complex × 2 (C6KST3) Proteasome subunit alpha type × 2 (Q8IDG3) Proteasome subunit alpha type × 2 (Q8IDG2) Proteasome endopeptidase complex × 2 (Q8IK90) Proteasome subunit alpha type-3, putative × 2 (O77396) Proteasome subunit beta type-6, putative × 2 (Q8I0U7) Proteasome subunit beta × 2 (Q8I6T3) Proteasome subunit beta × 2 (Q8I261) Proteasome subunit beta × 2 (Q8IKC9) Proteasome subunit beta type × 2 (Q8IJT1) Proteasome subunit beta × 2 Proteasome subunit beta × 2 (A0A5K1K7U1) A1B73 (3S)-1-({[(3S)-piperidin-3-yl]oxy}acetyl)-N-({4-[4-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl}methyl)piperidine-3-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8IBI3_PLAF7
Isoform
PDB entities 5
Chains and sequence ranges Author chain E; PDBConstruct 1–256; UniProt 1–256 Author chain S; PDBConstruct 1–256; UniProt 1–256

Proteasome endopeptidase complex

OrganismNot specified

UniProt Q8IK90

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain F; UniProt 1–254 Chain T; UniProt 1–254 Not recorded Proteasome endopeptidase complex × 2 (Q8IAR3) Proteasome endopeptidase complex × 2 (C6KST3) Proteasome subunit alpha type × 2 (Q8IDG3) Proteasome subunit alpha type × 2 (Q8IDG2) Proteasome subunit alpha type × 2 (Q8IBI3) Proteasome subunit alpha type-3, putative × 2 (O77396) Proteasome subunit beta type-6, putative × 2 (Q8I0U7) Proteasome subunit beta × 2 (Q8I6T3) Proteasome subunit beta × 2 (Q8I261) Proteasome subunit beta × 2 (Q8IKC9) Proteasome subunit beta type × 2 (Q8IJT1) Proteasome subunit beta × 2 Proteasome subunit beta × 2 (A0A5K1K7U1) A1B73 (3S)-1-({[(3S)-piperidin-3-yl]oxy}acetyl)-N-({4-[4-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl}methyl)piperidine-3-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8IK90_PLAF7
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–254; UniProt 1–254 Author chain T; PDBConstruct 1–254; UniProt 1–254

Proteasome subunit alpha type-3, putative

OrganismNot specified

UniProt O77396

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain G; UniProt 1–252 Chain U; UniProt 1–252 Not recorded Proteasome endopeptidase complex × 2 (Q8IAR3) Proteasome endopeptidase complex × 2 (C6KST3) Proteasome subunit alpha type × 2 (Q8IDG3) Proteasome subunit alpha type × 2 (Q8IDG2) Proteasome subunit alpha type × 2 (Q8IBI3) Proteasome endopeptidase complex × 2 (Q8IK90) Proteasome subunit beta type-6, putative × 2 (Q8I0U7) Proteasome subunit beta × 2 (Q8I6T3) Proteasome subunit beta × 2 (Q8I261) Proteasome subunit beta × 2 (Q8IKC9) Proteasome subunit beta type × 2 (Q8IJT1) Proteasome subunit beta × 2 Proteasome subunit beta × 2 (A0A5K1K7U1) A1B73 (3S)-1-({[(3S)-piperidin-3-yl]oxy}acetyl)-N-({4-[4-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl}methyl)piperidine-3-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O77396_PLAF7
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-6, putative

OrganismNot specified

UniProt Q8I0U7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain H; UniProt 31–282 Chain V; UniProt 31–282 Not recorded Proteasome endopeptidase complex × 2 (Q8IAR3) Proteasome endopeptidase complex × 2 (C6KST3) Proteasome subunit alpha type × 2 (Q8IDG3) Proteasome subunit alpha type × 2 (Q8IDG2) Proteasome subunit alpha type × 2 (Q8IBI3) Proteasome endopeptidase complex × 2 (Q8IK90) Proteasome subunit alpha type-3, putative × 2 (O77396) Proteasome subunit beta × 2 (Q8I6T3) Proteasome subunit beta × 2 (Q8I261) Proteasome subunit beta × 2 (Q8IKC9) Proteasome subunit beta type × 2 (Q8IJT1) Proteasome subunit beta × 2 Proteasome subunit beta × 2 (A0A5K1K7U1) A1B73 (3S)-1-({[(3S)-piperidin-3-yl]oxy}acetyl)-N-({4-[4-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl}methyl)piperidine-3-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8I0U7_PLAF7
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–252; UniProt 31–282 Author chain V; PDBConstruct 1–252; UniProt 31–282

Proteasome subunit beta

OrganismNot specified

UniProt Q8I6T3

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain I; UniProt 42–270 Chain W; UniProt 42–270 Not recorded Proteasome endopeptidase complex × 2 (Q8IAR3) Proteasome endopeptidase complex × 2 (C6KST3) Proteasome subunit alpha type × 2 (Q8IDG3) Proteasome subunit alpha type × 2 (Q8IDG2) Proteasome subunit alpha type × 2 (Q8IBI3) Proteasome endopeptidase complex × 2 (Q8IK90) Proteasome subunit alpha type-3, putative × 2 (O77396) Proteasome subunit beta type-6, putative × 2 (Q8I0U7) Proteasome subunit beta × 2 (Q8I261) Proteasome subunit beta × 2 (Q8IKC9) Proteasome subunit beta type × 2 (Q8IJT1) Proteasome subunit beta × 2 Proteasome subunit beta × 2 (A0A5K1K7U1) A1B73 (3S)-1-({[(3S)-piperidin-3-yl]oxy}acetyl)-N-({4-[4-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl}methyl)piperidine-3-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

12 other PDB entries and 12 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8I6T3_PLAF7
Isoform
PDB entities 9
Chains and sequence ranges Author chain I; PDBConstruct 1–229; UniProt 42–270 Author chain W; PDBConstruct 1–229; UniProt 42–270

Proteasome subunit beta

OrganismNot specified

UniProt Q8I261

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain J; UniProt 1–218 Chain X; UniProt 1–218 Not recorded Proteasome endopeptidase complex × 2 (Q8IAR3) Proteasome endopeptidase complex × 2 (C6KST3) Proteasome subunit alpha type × 2 (Q8IDG3) Proteasome subunit alpha type × 2 (Q8IDG2) Proteasome subunit alpha type × 2 (Q8IBI3) Proteasome endopeptidase complex × 2 (Q8IK90) Proteasome subunit alpha type-3, putative × 2 (O77396) Proteasome subunit beta type-6, putative × 2 (Q8I0U7) Proteasome subunit beta × 2 (Q8I6T3) Proteasome subunit beta × 2 (Q8IKC9) Proteasome subunit beta type × 2 (Q8IJT1) Proteasome subunit beta × 2 Proteasome subunit beta × 2 (A0A5K1K7U1) A1B73 (3S)-1-({[(3S)-piperidin-3-yl]oxy}acetyl)-N-({4-[4-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl}methyl)piperidine-3-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8I261_PLAF7
Isoform
PDB entities 10
Chains and sequence ranges Author chain J; PDBConstruct 1–218; UniProt 1–218 Author chain X; PDBConstruct 1–218; UniProt 1–218

Proteasome subunit beta

OrganismNot specified

UniProt Q8IKC9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain K; UniProt 1–195 Chain Y; UniProt 1–195 Not recorded Proteasome endopeptidase complex × 2 (Q8IAR3) Proteasome endopeptidase complex × 2 (C6KST3) Proteasome subunit alpha type × 2 (Q8IDG3) Proteasome subunit alpha type × 2 (Q8IDG2) Proteasome subunit alpha type × 2 (Q8IBI3) Proteasome endopeptidase complex × 2 (Q8IK90) Proteasome subunit alpha type-3, putative × 2 (O77396) Proteasome subunit beta type-6, putative × 2 (Q8I0U7) Proteasome subunit beta × 2 (Q8I6T3) Proteasome subunit beta × 2 (Q8I261) Proteasome subunit beta type × 2 (Q8IJT1) Proteasome subunit beta × 2 Proteasome subunit beta × 2 (A0A5K1K7U1) A1B73 (3S)-1-({[(3S)-piperidin-3-yl]oxy}acetyl)-N-({4-[4-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl}methyl)piperidine-3-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8IKC9_PLAF7
Isoform
PDB entities 11
Chains and sequence ranges Author chain K; PDBConstruct 1–195; UniProt 1–195 Author chain Y; PDBConstruct 1–195; UniProt 1–195

Proteasome subunit beta type

OrganismNot specified

UniProt Q8IJT1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain L; UniProt 61–271 Chain Z; UniProt 61–271 Not recorded Proteasome endopeptidase complex × 2 (Q8IAR3) Proteasome endopeptidase complex × 2 (C6KST3) Proteasome subunit alpha type × 2 (Q8IDG3) Proteasome subunit alpha type × 2 (Q8IDG2) Proteasome subunit alpha type × 2 (Q8IBI3) Proteasome endopeptidase complex × 2 (Q8IK90) Proteasome subunit alpha type-3, putative × 2 (O77396) Proteasome subunit beta type-6, putative × 2 (Q8I0U7) Proteasome subunit beta × 2 (Q8I6T3) Proteasome subunit beta × 2 (Q8I261) Proteasome subunit beta × 2 (Q8IKC9) Proteasome subunit beta × 2 Proteasome subunit beta × 2 (A0A5K1K7U1) A1B73 (3S)-1-({[(3S)-piperidin-3-yl]oxy}acetyl)-N-({4-[4-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl}methyl)piperidine-3-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q8IJT1_PLAF7
Isoform
PDB entities 12
Chains and sequence ranges Author chain L; PDBConstruct 1–211; UniProt 61–271 Author chain Z; PDBConstruct 1–211; UniProt 61–271

Proteasome subunit beta

OrganismNot specified

UniProt A0A5K1K7U1

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 28 PDB declaration: 28-meric(28) Consistent with protein copy count Chain M; UniProt 1–240 Chain a; UniProt 1–240 Not recorded Proteasome endopeptidase complex × 2 (Q8IAR3) Proteasome endopeptidase complex × 2 (C6KST3) Proteasome subunit alpha type × 2 (Q8IDG3) Proteasome subunit alpha type × 2 (Q8IDG2) Proteasome subunit alpha type × 2 (Q8IBI3) Proteasome endopeptidase complex × 2 (Q8IK90) Proteasome subunit alpha type-3, putative × 2 (O77396) Proteasome subunit beta type-6, putative × 2 (Q8I0U7) Proteasome subunit beta × 2 (Q8I6T3) Proteasome subunit beta × 2 (Q8I261) Proteasome subunit beta × 2 (Q8IKC9) Proteasome subunit beta type × 2 (Q8IJT1) Proteasome subunit beta × 2 A1B73 (3S)-1-({[(3S)-piperidin-3-yl]oxy}acetyl)-N-({4-[4-(trifluoromethyl)phenyl]-1,3-thiazol-2-yl}methyl)piperidine-3-carboxamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.28 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A5K1K7U1_PLAF7
Isoform
PDB entities 14
Chains and sequence ranges Author chain M; PDBConstruct 1–240; UniProt 1–240 Author chain a; PDBConstruct 1–240; UniProt 1–240

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 9o3f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9o3f
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9o3f
Deposition date deposition_date2025-04-07
Structure title titlePlasmodium falciparum 20S proteasome bound to inhibitor 296
Keywords keywordsMalaria, Plasmodium falciparum, proteasome, drug discovery, CYTOSOLIC PROTEIN, CYTOSOLIC PROTEIN-INHIBITOR complex; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.09
Radius of gyration Rg (electron density) rg_electron59.63
Forward intensity I(0) i013761700000.00
Molecular weight molecular_weight658790.0 kDa
Excluded volume excluded_volume638570 ų
Envelope volume envelope_volume1257800 ų
Hydration-shell volume shell_volume168800 ų
Envelope diameter envelope_diameter195.1
Shell Rg shell_rg67.90
Envelope Rg envelope_rg57.58
Shape Rg shape_rg59.62
Total Rg total_rg59.75
Total atoms total_atoms49857
Residues n_residues6247
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax187.3
Rg (real space) rg_real59.79
Rg uncertainty (real space) rg_real_error0.96
I(0) (real space) i0_real1.3760e+10
I(0) uncertainty (real space) i0_real_error2.6980e+08
Rg (reciprocal space) rg_reciprocal60.32
I(0) (reciprocal space) i0_reciprocal13770000000.0000
Solution quality estimate total_estimate0.8131
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary79.2
Skewness Skewness skewness0.196
Kurtosis Kurtosis kurtosis-0.433
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha893300000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.867; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.964; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (15)

8. Citations (1)

9. Files and Curves (10)