8g6e

Structure of the Plasmodium falciparum 20S proteasome complexed with inhibitor TDI-8304

Method: ELECTRON MICROSCOPY Dmax: 196.5 Å Quality: GOOD

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

Proteasome subunit alpha type-6

OrganismNot specified

UniProt W7JVP8

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 (A0A2I0BQ13) Proteasome subunit alpha type × 2 (W7KN95) Proteasome subunit alpha type × 2 (A0A2I0BS43) Proteasome subunit alpha type × 2 (A0A2I0BP34) Proteasome subunit alpha type-1 × 2 (W7K5W7) Proteasome subunit alpha type-3 × 2 (W7K040) Proteasome subunit beta type-6 × 2 (W7JUG8) Proteasome subunit beta × 2 (W7K1J4) Proteasome subunit beta × 2 (A0A2I0BXS0) Proteasome subunit beta × 2 (W7JKG5) Proteasome subunit beta × 2 (W7K6A8) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 (W7K6I2) YRE (7S,10S,13S)-N-cyclopentyl-10-[2-(morpholin-4-yl)ethyl]-9,12-dioxo-13-(2-oxopyrrolidin-1-yl)-2-oxa-8,11-diazabicyclo[13.3.1]nonadeca-1(19),15,17-triene-7-carboxamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.18 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 W7JVP8_PLAFO
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

OrganismNot specified

UniProt A0A2I0BQ13

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 (W7JVP8) Proteasome subunit alpha type × 2 (W7KN95) Proteasome subunit alpha type × 2 (A0A2I0BS43) Proteasome subunit alpha type × 2 (A0A2I0BP34) Proteasome subunit alpha type-1 × 2 (W7K5W7) Proteasome subunit alpha type-3 × 2 (W7K040) Proteasome subunit beta type-6 × 2 (W7JUG8) Proteasome subunit beta × 2 (W7K1J4) Proteasome subunit beta × 2 (A0A2I0BXS0) Proteasome subunit beta × 2 (W7JKG5) Proteasome subunit beta × 2 (W7K6A8) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 (W7K6I2) YRE (7S,10S,13S)-N-cyclopentyl-10-[2-(morpholin-4-yl)ethyl]-9,12-dioxo-13-(2-oxopyrrolidin-1-yl)-2-oxa-8,11-diazabicyclo[13.3.1]nonadeca-1(19),15,17-triene-7-carboxamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.18 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 A0A2I0BQ13_PLAFO
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 W7KN95

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 (W7JVP8) Proteasome subunit alpha type-2 × 2 (A0A2I0BQ13) Proteasome subunit alpha type × 2 (A0A2I0BS43) Proteasome subunit alpha type × 2 (A0A2I0BP34) Proteasome subunit alpha type-1 × 2 (W7K5W7) Proteasome subunit alpha type-3 × 2 (W7K040) Proteasome subunit beta type-6 × 2 (W7JUG8) Proteasome subunit beta × 2 (W7K1J4) Proteasome subunit beta × 2 (A0A2I0BXS0) Proteasome subunit beta × 2 (W7JKG5) Proteasome subunit beta × 2 (W7K6A8) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 (W7K6I2) YRE (7S,10S,13S)-N-cyclopentyl-10-[2-(morpholin-4-yl)ethyl]-9,12-dioxo-13-(2-oxopyrrolidin-1-yl)-2-oxa-8,11-diazabicyclo[13.3.1]nonadeca-1(19),15,17-triene-7-carboxamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.18 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 W7KN95_PLAFO
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

OrganismNot specified

UniProt A0A2I0BS43

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 (W7JVP8) Proteasome subunit alpha type-2 × 2 (A0A2I0BQ13) Proteasome subunit alpha type × 2 (W7KN95) Proteasome subunit alpha type × 2 (A0A2I0BP34) Proteasome subunit alpha type-1 × 2 (W7K5W7) Proteasome subunit alpha type-3 × 2 (W7K040) Proteasome subunit beta type-6 × 2 (W7JUG8) Proteasome subunit beta × 2 (W7K1J4) Proteasome subunit beta × 2 (A0A2I0BXS0) Proteasome subunit beta × 2 (W7JKG5) Proteasome subunit beta × 2 (W7K6A8) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 (W7K6I2) YRE (7S,10S,13S)-N-cyclopentyl-10-[2-(morpholin-4-yl)ethyl]-9,12-dioxo-13-(2-oxopyrrolidin-1-yl)-2-oxa-8,11-diazabicyclo[13.3.1]nonadeca-1(19),15,17-triene-7-carboxamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.18 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 A0A2I0BS43_PLAFO
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 A0A2I0BP34

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 (W7JVP8) Proteasome subunit alpha type-2 × 2 (A0A2I0BQ13) Proteasome subunit alpha type × 2 (W7KN95) Proteasome subunit alpha type × 2 (A0A2I0BS43) Proteasome subunit alpha type-1 × 2 (W7K5W7) Proteasome subunit alpha type-3 × 2 (W7K040) Proteasome subunit beta type-6 × 2 (W7JUG8) Proteasome subunit beta × 2 (W7K1J4) Proteasome subunit beta × 2 (A0A2I0BXS0) Proteasome subunit beta × 2 (W7JKG5) Proteasome subunit beta × 2 (W7K6A8) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 (W7K6I2) YRE (7S,10S,13S)-N-cyclopentyl-10-[2-(morpholin-4-yl)ethyl]-9,12-dioxo-13-(2-oxopyrrolidin-1-yl)-2-oxa-8,11-diazabicyclo[13.3.1]nonadeca-1(19),15,17-triene-7-carboxamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.18 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 A0A2I0BP34_PLAFO
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

OrganismNot specified

UniProt W7K5W7

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 1–253 Chain T; UniProt 1–253 Not recorded Proteasome subunit alpha type-6 × 2 (W7JVP8) Proteasome subunit alpha type-2 × 2 (A0A2I0BQ13) Proteasome subunit alpha type × 2 (W7KN95) Proteasome subunit alpha type × 2 (A0A2I0BS43) Proteasome subunit alpha type × 2 (A0A2I0BP34) Proteasome subunit alpha type-3 × 2 (W7K040) Proteasome subunit beta type-6 × 2 (W7JUG8) Proteasome subunit beta × 2 (W7K1J4) Proteasome subunit beta × 2 (A0A2I0BXS0) Proteasome subunit beta × 2 (W7JKG5) Proteasome subunit beta × 2 (W7K6A8) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 (W7K6I2) YRE (7S,10S,13S)-N-cyclopentyl-10-[2-(morpholin-4-yl)ethyl]-9,12-dioxo-13-(2-oxopyrrolidin-1-yl)-2-oxa-8,11-diazabicyclo[13.3.1]nonadeca-1(19),15,17-triene-7-carboxamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.18 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 W7K5W7_PLAFO
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–253; UniProt 1–253 Author chain T; PDBConstruct 1–253; UniProt 1–253

Proteasome subunit alpha type-3

OrganismNot specified

UniProt W7K040

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 (W7JVP8) Proteasome subunit alpha type-2 × 2 (A0A2I0BQ13) Proteasome subunit alpha type × 2 (W7KN95) Proteasome subunit alpha type × 2 (A0A2I0BS43) Proteasome subunit alpha type × 2 (A0A2I0BP34) Proteasome subunit alpha type-1 × 2 (W7K5W7) Proteasome subunit beta type-6 × 2 (W7JUG8) Proteasome subunit beta × 2 (W7K1J4) Proteasome subunit beta × 2 (A0A2I0BXS0) Proteasome subunit beta × 2 (W7JKG5) Proteasome subunit beta × 2 (W7K6A8) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 (W7K6I2) YRE (7S,10S,13S)-N-cyclopentyl-10-[2-(morpholin-4-yl)ethyl]-9,12-dioxo-13-(2-oxopyrrolidin-1-yl)-2-oxa-8,11-diazabicyclo[13.3.1]nonadeca-1(19),15,17-triene-7-carboxamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.18 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 W7K040_PLAFO
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

OrganismNot specified

UniProt W7JUG8

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 (W7JVP8) Proteasome subunit alpha type-2 × 2 (A0A2I0BQ13) Proteasome subunit alpha type × 2 (W7KN95) Proteasome subunit alpha type × 2 (A0A2I0BS43) Proteasome subunit alpha type × 2 (A0A2I0BP34) Proteasome subunit alpha type-1 × 2 (W7K5W7) Proteasome subunit alpha type-3 × 2 (W7K040) Proteasome subunit beta × 2 (W7K1J4) Proteasome subunit beta × 2 (A0A2I0BXS0) Proteasome subunit beta × 2 (W7JKG5) Proteasome subunit beta × 2 (W7K6A8) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 (W7K6I2) YRE (7S,10S,13S)-N-cyclopentyl-10-[2-(morpholin-4-yl)ethyl]-9,12-dioxo-13-(2-oxopyrrolidin-1-yl)-2-oxa-8,11-diazabicyclo[13.3.1]nonadeca-1(19),15,17-triene-7-carboxamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.18 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 W7JUG8_PLAFO
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 W7K1J4

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 (W7JVP8) Proteasome subunit alpha type-2 × 2 (A0A2I0BQ13) Proteasome subunit alpha type × 2 (W7KN95) Proteasome subunit alpha type × 2 (A0A2I0BS43) Proteasome subunit alpha type × 2 (A0A2I0BP34) Proteasome subunit alpha type-1 × 2 (W7K5W7) Proteasome subunit alpha type-3 × 2 (W7K040) Proteasome subunit beta type-6 × 2 (W7JUG8) Proteasome subunit beta × 2 (A0A2I0BXS0) Proteasome subunit beta × 2 (W7JKG5) Proteasome subunit beta × 2 (W7K6A8) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 (W7K6I2) YRE (7S,10S,13S)-N-cyclopentyl-10-[2-(morpholin-4-yl)ethyl]-9,12-dioxo-13-(2-oxopyrrolidin-1-yl)-2-oxa-8,11-diazabicyclo[13.3.1]nonadeca-1(19),15,17-triene-7-carboxamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.18 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name W7K1J4_PLAFO
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 A0A2I0BXS0

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 (W7JVP8) Proteasome subunit alpha type-2 × 2 (A0A2I0BQ13) Proteasome subunit alpha type × 2 (W7KN95) Proteasome subunit alpha type × 2 (A0A2I0BS43) Proteasome subunit alpha type × 2 (A0A2I0BP34) Proteasome subunit alpha type-1 × 2 (W7K5W7) Proteasome subunit alpha type-3 × 2 (W7K040) Proteasome subunit beta type-6 × 2 (W7JUG8) Proteasome subunit beta × 2 (W7K1J4) Proteasome subunit beta × 2 (W7JKG5) Proteasome subunit beta × 2 (W7K6A8) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 (W7K6I2) YRE (7S,10S,13S)-N-cyclopentyl-10-[2-(morpholin-4-yl)ethyl]-9,12-dioxo-13-(2-oxopyrrolidin-1-yl)-2-oxa-8,11-diazabicyclo[13.3.1]nonadeca-1(19),15,17-triene-7-carboxamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.18 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 A0A2I0BXS0_PLAFO
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 W7JKG5

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 (W7JVP8) Proteasome subunit alpha type-2 × 2 (A0A2I0BQ13) Proteasome subunit alpha type × 2 (W7KN95) Proteasome subunit alpha type × 2 (A0A2I0BS43) Proteasome subunit alpha type × 2 (A0A2I0BP34) Proteasome subunit alpha type-1 × 2 (W7K5W7) Proteasome subunit alpha type-3 × 2 (W7K040) Proteasome subunit beta type-6 × 2 (W7JUG8) Proteasome subunit beta × 2 (W7K1J4) Proteasome subunit beta × 2 (A0A2I0BXS0) Proteasome subunit beta × 2 (W7K6A8) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 (W7K6I2) YRE (7S,10S,13S)-N-cyclopentyl-10-[2-(morpholin-4-yl)ethyl]-9,12-dioxo-13-(2-oxopyrrolidin-1-yl)-2-oxa-8,11-diazabicyclo[13.3.1]nonadeca-1(19),15,17-triene-7-carboxamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.18 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 W7JKG5_PLAFO
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

OrganismNot specified

UniProt W7K6A8

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 subunit alpha type-6 × 2 (W7JVP8) Proteasome subunit alpha type-2 × 2 (A0A2I0BQ13) Proteasome subunit alpha type × 2 (W7KN95) Proteasome subunit alpha type × 2 (A0A2I0BS43) Proteasome subunit alpha type × 2 (A0A2I0BP34) Proteasome subunit alpha type-1 × 2 (W7K5W7) Proteasome subunit alpha type-3 × 2 (W7K040) Proteasome subunit beta type-6 × 2 (W7JUG8) Proteasome subunit beta × 2 (W7K1J4) Proteasome subunit beta × 2 (A0A2I0BXS0) Proteasome subunit beta × 2 (W7JKG5) Proteasome subunit beta × 2 (A0A2I0BU46) Proteasome subunit beta × 2 (W7K6I2) YRE (7S,10S,13S)-N-cyclopentyl-10-[2-(morpholin-4-yl)ethyl]-9,12-dioxo-13-(2-oxopyrrolidin-1-yl)-2-oxa-8,11-diazabicyclo[13.3.1]nonadeca-1(19),15,17-triene-7-carboxamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.18 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name W7K6A8_PLAFO
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 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 (W7JVP8) Proteasome subunit alpha type-2 × 2 (A0A2I0BQ13) Proteasome subunit alpha type × 2 (W7KN95) Proteasome subunit alpha type × 2 (A0A2I0BS43) Proteasome subunit alpha type × 2 (A0A2I0BP34) Proteasome subunit alpha type-1 × 2 (W7K5W7) Proteasome subunit alpha type-3 × 2 (W7K040) Proteasome subunit beta type-6 × 2 (W7JUG8) Proteasome subunit beta × 2 (W7K1J4) Proteasome subunit beta × 2 (A0A2I0BXS0) Proteasome subunit beta × 2 (W7JKG5) Proteasome subunit beta × 2 (W7K6A8) Proteasome subunit beta × 2 (W7K6I2) YRE (7S,10S,13S)-N-cyclopentyl-10-[2-(morpholin-4-yl)ethyl]-9,12-dioxo-13-(2-oxopyrrolidin-1-yl)-2-oxa-8,11-diazabicyclo[13.3.1]nonadeca-1(19),15,17-triene-7-carboxamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.18 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

Proteasome subunit beta

OrganismNot specified

UniProt W7K6I2

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 N; UniProt 1–265 Chain b; UniProt 1–265 Not recorded Proteasome subunit alpha type-6 × 2 (W7JVP8) Proteasome subunit alpha type-2 × 2 (A0A2I0BQ13) Proteasome subunit alpha type × 2 (W7KN95) Proteasome subunit alpha type × 2 (A0A2I0BS43) Proteasome subunit alpha type × 2 (A0A2I0BP34) Proteasome subunit alpha type-1 × 2 (W7K5W7) Proteasome subunit alpha type-3 × 2 (W7K040) Proteasome subunit beta type-6 × 2 (W7JUG8) Proteasome subunit beta × 2 (W7K1J4) Proteasome subunit beta × 2 (A0A2I0BXS0) Proteasome subunit beta × 2 (W7JKG5) Proteasome subunit beta × 2 (W7K6A8) Proteasome subunit beta × 2 (A0A2I0BU46) YRE (7S,10S,13S)-N-cyclopentyl-10-[2-(morpholin-4-yl)ethyl]-9,12-dioxo-13-(2-oxopyrrolidin-1-yl)-2-oxa-8,11-diazabicyclo[13.3.1]nonadeca-1(19),15,17-triene-7-carboxamide × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.18 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 W7K6I2_PLAFO
Isoform
PDB entities 14
Chains and sequence ranges Author chain N; PDBConstruct 1–265; UniProt 1–265 Author chain b; PDBConstruct 1–265; UniProt 1–265

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 8g6e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8g6e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8g6e
Deposition date deposition_date2023-02-15
Structure title titleStructure of the Plasmodium falciparum 20S proteasome complexed with inhibitor TDI-8304
Keywords keywordsproteasome, inhibitor, 20S, HYDROLASE, HYDROLASE-HYDROLASE INHIBITOR complex; HYDROLASE/HYDROLASE INHIBITOR
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.25
Radius of gyration Rg (electron density) rg_electron59.76
Forward intensity I(0) i07400530000.00
Molecular weight molecular_weight739420.0 kDa
Excluded volume excluded_volume929780 ų
Envelope volume envelope_volume1292800 ų
Hydration-shell volume shell_volume172050 ų
Envelope diameter envelope_diameter197.3
Shell Rg shell_rg68.54
Envelope Rg envelope_rg58.00
Shape Rg shape_rg59.73
Total Rg total_rg60.03
Total atoms total_atoms52006
Residues n_residues6490
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 dmax196.5
Rg (real space) rg_real59.94
Rg uncertainty (real space) rg_real_error1.60
I(0) (real space) i0_real7.4000e+09
I(0) uncertainty (real space) i0_real_error1.6970e+08
Rg (reciprocal space) rg_reciprocal60.48
I(0) (reciprocal space) i0_reciprocal7407000000.0000
Solution quality estimate total_estimate0.8597
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary75.6
Skewness Skewness skewness0.196
Kurtosis Kurtosis kurtosis-0.417
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1209000000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.796; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.950; Smooth: 0.835

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (16)

8. Citations (1)

9. Files and Curves (10)