9y0k

Structure of Plasmodium falciparum 20S proteasome with bound J80

Method: ELECTRON MICROSCOPY Dmax: 189.0 Å Quality: GOOD

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

Proteasome subunit alpha type-6

Plasmodium falciparum Dd2

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 subunit alpha type-2 × 2 (C6KST3) Proteasome subunit alpha type-3 × 2 (Q8IDG3) Proteasome subunit alpha type-4 × 2 (Q8IDG2) Proteasome subunit alpha type-5 × 2 (A0A0L7LVZ5) Proteasome subunit alpha type-1 × 2 (Q8IK90) Proteasome subunit alpha type-3 × 2 (O77396) Proteasome endopeptidase complex × 2 (A0A0L7M1M6) Proteasome subunit beta-2 × 2 (Q8I6T3) Proteasome subunit beta-3 × 2 (Q8I261) Proteasome subunit beta-4 × 2 (Q8IKC9) Proteasome subunit beta × 2 (A0A024W8G7) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 A1CRO N,N-diethyl-N~2~-hexanoyl-D-asparaginyl-N-{(1S)-2-(2,4-difluorophenyl)-1-[(2S,3S,5S,6S)-5-formyl-2-hydroxy-3-(hydroxymethyl)-3,6-dimethylmorpholin-2-yl]ethyl}-4-fluoro-L-phenylalaninamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 subunit alpha type-2

Plasmodium falciparum Dd2

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 subunit alpha type-6 × 2 (Q8IAR3) Proteasome subunit alpha type-3 × 2 (Q8IDG3) Proteasome subunit alpha type-4 × 2 (Q8IDG2) Proteasome subunit alpha type-5 × 2 (A0A0L7LVZ5) Proteasome subunit alpha type-1 × 2 (Q8IK90) Proteasome subunit alpha type-3 × 2 (O77396) Proteasome endopeptidase complex × 2 (A0A0L7M1M6) Proteasome subunit beta-2 × 2 (Q8I6T3) Proteasome subunit beta-3 × 2 (Q8I261) Proteasome subunit beta-4 × 2 (Q8IKC9) Proteasome subunit beta × 2 (A0A024W8G7) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 A1CRO N,N-diethyl-N~2~-hexanoyl-D-asparaginyl-N-{(1S)-2-(2,4-difluorophenyl)-1-[(2S,3S,5S,6S)-5-formyl-2-hydroxy-3-(hydroxymethyl)-3,6-dimethylmorpholin-2-yl]ethyl}-4-fluoro-L-phenylalaninamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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-3

Plasmodium falciparum Dd2

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 1–246 Chain Q; UniProt 1–246 Not recorded Proteasome subunit alpha type-6 × 2 (Q8IAR3) Proteasome subunit alpha type-2 × 2 (C6KST3) Proteasome subunit alpha type-4 × 2 (Q8IDG2) Proteasome subunit alpha type-5 × 2 (A0A0L7LVZ5) Proteasome subunit alpha type-1 × 2 (Q8IK90) Proteasome subunit alpha type-3 × 2 (O77396) Proteasome endopeptidase complex × 2 (A0A0L7M1M6) Proteasome subunit beta-2 × 2 (Q8I6T3) Proteasome subunit beta-3 × 2 (Q8I261) Proteasome subunit beta-4 × 2 (Q8IKC9) Proteasome subunit beta × 2 (A0A024W8G7) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 A1CRO N,N-diethyl-N~2~-hexanoyl-D-asparaginyl-N-{(1S)-2-(2,4-difluorophenyl)-1-[(2S,3S,5S,6S)-5-formyl-2-hydroxy-3-(hydroxymethyl)-3,6-dimethylmorpholin-2-yl]ethyl}-4-fluoro-L-phenylalaninamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 1–246; UniProt 1–246 Author chain Q; PDBConstruct 1–246; UniProt 1–246

Proteasome subunit alpha type-4

Plasmodium falciparum Dd2

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 subunit alpha type-6 × 2 (Q8IAR3) Proteasome subunit alpha type-2 × 2 (C6KST3) Proteasome subunit alpha type-3 × 2 (Q8IDG3) Proteasome subunit alpha type-5 × 2 (A0A0L7LVZ5) Proteasome subunit alpha type-1 × 2 (Q8IK90) Proteasome subunit alpha type-3 × 2 (O77396) Proteasome endopeptidase complex × 2 (A0A0L7M1M6) Proteasome subunit beta-2 × 2 (Q8I6T3) Proteasome subunit beta-3 × 2 (Q8I261) Proteasome subunit beta-4 × 2 (Q8IKC9) Proteasome subunit beta × 2 (A0A024W8G7) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 A1CRO N,N-diethyl-N~2~-hexanoyl-D-asparaginyl-N-{(1S)-2-(2,4-difluorophenyl)-1-[(2S,3S,5S,6S)-5-formyl-2-hydroxy-3-(hydroxymethyl)-3,6-dimethylmorpholin-2-yl]ethyl}-4-fluoro-L-phenylalaninamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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-5

Plasmodium falciparum Dd2

UniProt A0A0L7LVZ5

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 subunit alpha type-6 × 2 (Q8IAR3) Proteasome subunit alpha type-2 × 2 (C6KST3) Proteasome subunit alpha type-3 × 2 (Q8IDG3) Proteasome subunit alpha type-4 × 2 (Q8IDG2) Proteasome subunit alpha type-1 × 2 (Q8IK90) Proteasome subunit alpha type-3 × 2 (O77396) Proteasome endopeptidase complex × 2 (A0A0L7M1M6) Proteasome subunit beta-2 × 2 (Q8I6T3) Proteasome subunit beta-3 × 2 (Q8I261) Proteasome subunit beta-4 × 2 (Q8IKC9) Proteasome subunit beta × 2 (A0A024W8G7) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 A1CRO N,N-diethyl-N~2~-hexanoyl-D-asparaginyl-N-{(1S)-2-(2,4-difluorophenyl)-1-[(2S,3S,5S,6S)-5-formyl-2-hydroxy-3-(hydroxymethyl)-3,6-dimethylmorpholin-2-yl]ethyl}-4-fluoro-L-phenylalaninamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0L7LVZ5_PLAF4
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 subunit alpha type-1

Plasmodium falciparum Dd2

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 subunit alpha type-6 × 2 (Q8IAR3) Proteasome subunit alpha type-2 × 2 (C6KST3) Proteasome subunit alpha type-3 × 2 (Q8IDG3) Proteasome subunit alpha type-4 × 2 (Q8IDG2) Proteasome subunit alpha type-5 × 2 (A0A0L7LVZ5) Proteasome subunit alpha type-3 × 2 (O77396) Proteasome endopeptidase complex × 2 (A0A0L7M1M6) Proteasome subunit beta-2 × 2 (Q8I6T3) Proteasome subunit beta-3 × 2 (Q8I261) Proteasome subunit beta-4 × 2 (Q8IKC9) Proteasome subunit beta × 2 (A0A024W8G7) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 A1CRO N,N-diethyl-N~2~-hexanoyl-D-asparaginyl-N-{(1S)-2-(2,4-difluorophenyl)-1-[(2S,3S,5S,6S)-5-formyl-2-hydroxy-3-(hydroxymethyl)-3,6-dimethylmorpholin-2-yl]ethyl}-4-fluoro-L-phenylalaninamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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

Plasmodium falciparum Dd2

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 subunit alpha type-6 × 2 (Q8IAR3) Proteasome subunit alpha type-2 × 2 (C6KST3) Proteasome subunit alpha type-3 × 2 (Q8IDG3) Proteasome subunit alpha type-4 × 2 (Q8IDG2) Proteasome subunit alpha type-5 × 2 (A0A0L7LVZ5) Proteasome subunit alpha type-1 × 2 (Q8IK90) Proteasome endopeptidase complex × 2 (A0A0L7M1M6) Proteasome subunit beta-2 × 2 (Q8I6T3) Proteasome subunit beta-3 × 2 (Q8I261) Proteasome subunit beta-4 × 2 (Q8IKC9) Proteasome subunit beta × 2 (A0A024W8G7) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 A1CRO N,N-diethyl-N~2~-hexanoyl-D-asparaginyl-N-{(1S)-2-(2,4-difluorophenyl)-1-[(2S,3S,5S,6S)-5-formyl-2-hydroxy-3-(hydroxymethyl)-3,6-dimethylmorpholin-2-yl]ethyl}-4-fluoro-L-phenylalaninamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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 endopeptidase complex

Plasmodium falciparum Dd2

UniProt A0A0L7M1M6

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 subunit alpha type-6 × 2 (Q8IAR3) Proteasome subunit alpha type-2 × 2 (C6KST3) Proteasome subunit alpha type-3 × 2 (Q8IDG3) Proteasome subunit alpha type-4 × 2 (Q8IDG2) Proteasome subunit alpha type-5 × 2 (A0A0L7LVZ5) Proteasome subunit alpha type-1 × 2 (Q8IK90) Proteasome subunit alpha type-3 × 2 (O77396) Proteasome subunit beta-2 × 2 (Q8I6T3) Proteasome subunit beta-3 × 2 (Q8I261) Proteasome subunit beta-4 × 2 (Q8IKC9) Proteasome subunit beta × 2 (A0A024W8G7) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 A1CRO N,N-diethyl-N~2~-hexanoyl-D-asparaginyl-N-{(1S)-2-(2,4-difluorophenyl)-1-[(2S,3S,5S,6S)-5-formyl-2-hydroxy-3-(hydroxymethyl)-3,6-dimethylmorpholin-2-yl]ethyl}-4-fluoro-L-phenylalaninamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A0L7M1M6_PLAF4
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-2

Plasmodium falciparum Dd2

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 subunit alpha type-6 × 2 (Q8IAR3) Proteasome subunit alpha type-2 × 2 (C6KST3) Proteasome subunit alpha type-3 × 2 (Q8IDG3) Proteasome subunit alpha type-4 × 2 (Q8IDG2) Proteasome subunit alpha type-5 × 2 (A0A0L7LVZ5) Proteasome subunit alpha type-1 × 2 (Q8IK90) Proteasome subunit alpha type-3 × 2 (O77396) Proteasome endopeptidase complex × 2 (A0A0L7M1M6) Proteasome subunit beta-3 × 2 (Q8I261) Proteasome subunit beta-4 × 2 (Q8IKC9) Proteasome subunit beta × 2 (A0A024W8G7) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 A1CRO N,N-diethyl-N~2~-hexanoyl-D-asparaginyl-N-{(1S)-2-(2,4-difluorophenyl)-1-[(2S,3S,5S,6S)-5-formyl-2-hydroxy-3-(hydroxymethyl)-3,6-dimethylmorpholin-2-yl]ethyl}-4-fluoro-L-phenylalaninamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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-3

Plasmodium falciparum Dd2

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 subunit alpha type-6 × 2 (Q8IAR3) Proteasome subunit alpha type-2 × 2 (C6KST3) Proteasome subunit alpha type-3 × 2 (Q8IDG3) Proteasome subunit alpha type-4 × 2 (Q8IDG2) Proteasome subunit alpha type-5 × 2 (A0A0L7LVZ5) Proteasome subunit alpha type-1 × 2 (Q8IK90) Proteasome subunit alpha type-3 × 2 (O77396) Proteasome endopeptidase complex × 2 (A0A0L7M1M6) Proteasome subunit beta-2 × 2 (Q8I6T3) Proteasome subunit beta-4 × 2 (Q8IKC9) Proteasome subunit beta × 2 (A0A024W8G7) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 A1CRO N,N-diethyl-N~2~-hexanoyl-D-asparaginyl-N-{(1S)-2-(2,4-difluorophenyl)-1-[(2S,3S,5S,6S)-5-formyl-2-hydroxy-3-(hydroxymethyl)-3,6-dimethylmorpholin-2-yl]ethyl}-4-fluoro-L-phenylalaninamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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-4

Plasmodium falciparum Dd2

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 subunit alpha type-6 × 2 (Q8IAR3) Proteasome subunit alpha type-2 × 2 (C6KST3) Proteasome subunit alpha type-3 × 2 (Q8IDG3) Proteasome subunit alpha type-4 × 2 (Q8IDG2) Proteasome subunit alpha type-5 × 2 (A0A0L7LVZ5) Proteasome subunit alpha type-1 × 2 (Q8IK90) Proteasome subunit alpha type-3 × 2 (O77396) Proteasome endopeptidase complex × 2 (A0A0L7M1M6) Proteasome subunit beta-2 × 2 (Q8I6T3) Proteasome subunit beta-3 × 2 (Q8I261) Proteasome subunit beta × 2 (A0A024W8G7) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 A1CRO N,N-diethyl-N~2~-hexanoyl-D-asparaginyl-N-{(1S)-2-(2,4-difluorophenyl)-1-[(2S,3S,5S,6S)-5-formyl-2-hydroxy-3-(hydroxymethyl)-3,6-dimethylmorpholin-2-yl]ethyl}-4-fluoro-L-phenylalaninamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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

Plasmodium falciparum Dd2

UniProt A0A024W8G7

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 53–262 Chain Z; UniProt 53–262 Not recorded Proteasome subunit alpha type-6 × 2 (Q8IAR3) Proteasome subunit alpha type-2 × 2 (C6KST3) Proteasome subunit alpha type-3 × 2 (Q8IDG3) Proteasome subunit alpha type-4 × 2 (Q8IDG2) Proteasome subunit alpha type-5 × 2 (A0A0L7LVZ5) Proteasome subunit alpha type-1 × 2 (Q8IK90) Proteasome subunit alpha type-3 × 2 (O77396) Proteasome endopeptidase complex × 2 (A0A0L7M1M6) Proteasome subunit beta-2 × 2 (Q8I6T3) Proteasome subunit beta-3 × 2 (Q8I261) Proteasome subunit beta-4 × 2 (Q8IKC9) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 A1CRO N,N-diethyl-N~2~-hexanoyl-D-asparaginyl-N-{(1S)-2-(2,4-difluorophenyl)-1-[(2S,3S,5S,6S)-5-formyl-2-hydroxy-3-(hydroxymethyl)-3,6-dimethylmorpholin-2-yl]ethyl}-4-fluoro-L-phenylalaninamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name A0A024W8G7_PLAFA
Isoform
PDB entities 12
Chains and sequence ranges Author chain L; PDBConstruct 1–210; UniProt 53–262 Author chain Z; PDBConstruct 1–210; UniProt 53–262

Proteasome subunit beta

Plasmodium falciparum Dd2

UniProt A0A2I0BU46

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 subunit alpha type-6 × 2 (Q8IAR3) Proteasome subunit alpha type-2 × 2 (C6KST3) Proteasome subunit alpha type-3 × 2 (Q8IDG3) Proteasome subunit alpha type-4 × 2 (Q8IDG2) Proteasome subunit alpha type-5 × 2 (A0A0L7LVZ5) Proteasome subunit alpha type-1 × 2 (Q8IK90) Proteasome subunit alpha type-3 × 2 (O77396) Proteasome endopeptidase complex × 2 (A0A0L7M1M6) Proteasome subunit beta-2 × 2 (Q8I6T3) Proteasome subunit beta-3 × 2 (Q8I261) Proteasome subunit beta-4 × 2 (Q8IKC9) Proteasome subunit beta × 2 (A0A024W8G7) Proteasome subunit beta × 2 A1CRO N,N-diethyl-N~2~-hexanoyl-D-asparaginyl-N-{(1S)-2-(2,4-difluorophenyl)-1-[(2S,3S,5S,6S)-5-formyl-2-hydroxy-3-(hydroxymethyl)-3,6-dimethylmorpholin-2-yl]ethyl}-4-fluoro-L-phenylalaninamide × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.00 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A2I0BU46_PLAFO
Isoform
PDB entities 13
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 9y0k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9y0k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9y0k
Deposition date deposition_date2025-08-28
Structure title titleStructure of Plasmodium falciparum 20S proteasome with bound J80
Keywords keywordsProteasome, 20S proteasome, Plasmodium falciparum, proteasome inhibitor, HYDROLASE-INHIBITOR complex; HYDROLASE/INHIBITOR
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.03
Radius of gyration Rg (electron density) rg_electron59.58
Forward intensity I(0) i012736100000.00
Molecular weight molecular_weight636200.0 kDa
Excluded volume excluded_volume618100 ų
Envelope volume envelope_volume1242700 ų
Hydration-shell volume shell_volume167350 ų
Envelope diameter envelope_diameter193.4
Shell Rg shell_rg67.59
Envelope Rg envelope_rg57.41
Shape Rg shape_rg59.58
Total Rg total_rg59.70
Total atoms total_atoms48226
Residues n_residues6248
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 dmax189.0
Rg (real space) rg_real59.73
Rg uncertainty (real space) rg_real_error1.74
I(0) (real space) i0_real1.2740e+10
I(0) uncertainty (real space) i0_real_error2.7330e+08
Rg (reciprocal space) rg_reciprocal60.26
I(0) (reciprocal space) i0_reciprocal12750000000.0000
Solution quality estimate total_estimate0.8099
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary80.0
Skewness Skewness skewness0.192
Kurtosis Kurtosis kurtosis-0.436
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha886000000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.855; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.961; 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)