6muw

The structure of the Plasmodium falciparum 20S proteasome.

Method: ELECTRON MICROSCOPY Dmax: 173.1 Å Quality: GOOD

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

20S proteasome alpha-1 subunit

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 20S proteasome alpha-2 subunit × 2 (C6KST3) 20S proteasome alpha-3 subunit × 2 (Q8IDG3) 20S proteasome alpha-4 subunit × 2 (Q8IDG2) 20S proteasome alpha-5 subunit × 2 (Q8IBI3) 20S proteasome alpha-6 subunit × 2 (Q8IK90) 20S proteasome alpha-7 subunit × 2 (O77396) 20S proteasome beta-1 subunit × 2 (Q8I0U7) 20S proteasome beta-2 subunit × 2 (Q8I6T3) 20S proteasome beta-3 subunit × 2 (Q8I261) 20S proteasome beta-4 subunit × 2 (Q8IKC9) 20S proteasome beta-5 subunit × 2 (Q8IJT1) 20S proteasome beta-6 subunit × 2 (C0H4E8) 20S proteasome beta-7 subunit × 2 (Q7K6A9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;wait time 0sec blot time 2sec blot force -1 Resolution 3.60 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

20S proteasome alpha-2 subunit

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 20S proteasome alpha-1 subunit × 2 (Q8IAR3) 20S proteasome alpha-3 subunit × 2 (Q8IDG3) 20S proteasome alpha-4 subunit × 2 (Q8IDG2) 20S proteasome alpha-5 subunit × 2 (Q8IBI3) 20S proteasome alpha-6 subunit × 2 (Q8IK90) 20S proteasome alpha-7 subunit × 2 (O77396) 20S proteasome beta-1 subunit × 2 (Q8I0U7) 20S proteasome beta-2 subunit × 2 (Q8I6T3) 20S proteasome beta-3 subunit × 2 (Q8I261) 20S proteasome beta-4 subunit × 2 (Q8IKC9) 20S proteasome beta-5 subunit × 2 (Q8IJT1) 20S proteasome beta-6 subunit × 2 (C0H4E8) 20S proteasome beta-7 subunit × 2 (Q7K6A9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;wait time 0sec blot time 2sec blot force -1 Resolution 3.60 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

20S proteasome alpha-3 subunit

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 1–246 Chain Q; UniProt 1–246 Not recorded 20S proteasome alpha-1 subunit × 2 (Q8IAR3) 20S proteasome alpha-2 subunit × 2 (C6KST3) 20S proteasome alpha-4 subunit × 2 (Q8IDG2) 20S proteasome alpha-5 subunit × 2 (Q8IBI3) 20S proteasome alpha-6 subunit × 2 (Q8IK90) 20S proteasome alpha-7 subunit × 2 (O77396) 20S proteasome beta-1 subunit × 2 (Q8I0U7) 20S proteasome beta-2 subunit × 2 (Q8I6T3) 20S proteasome beta-3 subunit × 2 (Q8I261) 20S proteasome beta-4 subunit × 2 (Q8IKC9) 20S proteasome beta-5 subunit × 2 (Q8IJT1) 20S proteasome beta-6 subunit × 2 (C0H4E8) 20S proteasome beta-7 subunit × 2 (Q7K6A9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;wait time 0sec blot time 2sec blot force -1 Resolution 3.60 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

20S proteasome alpha-4 subunit

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 20S proteasome alpha-1 subunit × 2 (Q8IAR3) 20S proteasome alpha-2 subunit × 2 (C6KST3) 20S proteasome alpha-3 subunit × 2 (Q8IDG3) 20S proteasome alpha-5 subunit × 2 (Q8IBI3) 20S proteasome alpha-6 subunit × 2 (Q8IK90) 20S proteasome alpha-7 subunit × 2 (O77396) 20S proteasome beta-1 subunit × 2 (Q8I0U7) 20S proteasome beta-2 subunit × 2 (Q8I6T3) 20S proteasome beta-3 subunit × 2 (Q8I261) 20S proteasome beta-4 subunit × 2 (Q8IKC9) 20S proteasome beta-5 subunit × 2 (Q8IJT1) 20S proteasome beta-6 subunit × 2 (C0H4E8) 20S proteasome beta-7 subunit × 2 (Q7K6A9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;wait time 0sec blot time 2sec blot force -1 Resolution 3.60 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

20S proteasome alpha-5 subunit

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 20S proteasome alpha-1 subunit × 2 (Q8IAR3) 20S proteasome alpha-2 subunit × 2 (C6KST3) 20S proteasome alpha-3 subunit × 2 (Q8IDG3) 20S proteasome alpha-4 subunit × 2 (Q8IDG2) 20S proteasome alpha-6 subunit × 2 (Q8IK90) 20S proteasome alpha-7 subunit × 2 (O77396) 20S proteasome beta-1 subunit × 2 (Q8I0U7) 20S proteasome beta-2 subunit × 2 (Q8I6T3) 20S proteasome beta-3 subunit × 2 (Q8I261) 20S proteasome beta-4 subunit × 2 (Q8IKC9) 20S proteasome beta-5 subunit × 2 (Q8IJT1) 20S proteasome beta-6 subunit × 2 (C0H4E8) 20S proteasome beta-7 subunit × 2 (Q7K6A9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;wait time 0sec blot time 2sec blot force -1 Resolution 3.60 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

20S proteasome alpha-6 subunit

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 20S proteasome alpha-1 subunit × 2 (Q8IAR3) 20S proteasome alpha-2 subunit × 2 (C6KST3) 20S proteasome alpha-3 subunit × 2 (Q8IDG3) 20S proteasome alpha-4 subunit × 2 (Q8IDG2) 20S proteasome alpha-5 subunit × 2 (Q8IBI3) 20S proteasome alpha-7 subunit × 2 (O77396) 20S proteasome beta-1 subunit × 2 (Q8I0U7) 20S proteasome beta-2 subunit × 2 (Q8I6T3) 20S proteasome beta-3 subunit × 2 (Q8I261) 20S proteasome beta-4 subunit × 2 (Q8IKC9) 20S proteasome beta-5 subunit × 2 (Q8IJT1) 20S proteasome beta-6 subunit × 2 (C0H4E8) 20S proteasome beta-7 subunit × 2 (Q7K6A9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;wait time 0sec blot time 2sec blot force -1 Resolution 3.60 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

20S proteasome alpha-7 subunit

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 20S proteasome alpha-1 subunit × 2 (Q8IAR3) 20S proteasome alpha-2 subunit × 2 (C6KST3) 20S proteasome alpha-3 subunit × 2 (Q8IDG3) 20S proteasome alpha-4 subunit × 2 (Q8IDG2) 20S proteasome alpha-5 subunit × 2 (Q8IBI3) 20S proteasome alpha-6 subunit × 2 (Q8IK90) 20S proteasome beta-1 subunit × 2 (Q8I0U7) 20S proteasome beta-2 subunit × 2 (Q8I6T3) 20S proteasome beta-3 subunit × 2 (Q8I261) 20S proteasome beta-4 subunit × 2 (Q8IKC9) 20S proteasome beta-5 subunit × 2 (Q8IJT1) 20S proteasome beta-6 subunit × 2 (C0H4E8) 20S proteasome beta-7 subunit × 2 (Q7K6A9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;wait time 0sec blot time 2sec blot force -1 Resolution 3.60 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

20S proteasome beta-1 subunit

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 20S proteasome alpha-1 subunit × 2 (Q8IAR3) 20S proteasome alpha-2 subunit × 2 (C6KST3) 20S proteasome alpha-3 subunit × 2 (Q8IDG3) 20S proteasome alpha-4 subunit × 2 (Q8IDG2) 20S proteasome alpha-5 subunit × 2 (Q8IBI3) 20S proteasome alpha-6 subunit × 2 (Q8IK90) 20S proteasome alpha-7 subunit × 2 (O77396) 20S proteasome beta-2 subunit × 2 (Q8I6T3) 20S proteasome beta-3 subunit × 2 (Q8I261) 20S proteasome beta-4 subunit × 2 (Q8IKC9) 20S proteasome beta-5 subunit × 2 (Q8IJT1) 20S proteasome beta-6 subunit × 2 (C0H4E8) 20S proteasome beta-7 subunit × 2 (Q7K6A9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;wait time 0sec blot time 2sec blot force -1 Resolution 3.60 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

20S proteasome beta-2 subunit

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 20S proteasome alpha-1 subunit × 2 (Q8IAR3) 20S proteasome alpha-2 subunit × 2 (C6KST3) 20S proteasome alpha-3 subunit × 2 (Q8IDG3) 20S proteasome alpha-4 subunit × 2 (Q8IDG2) 20S proteasome alpha-5 subunit × 2 (Q8IBI3) 20S proteasome alpha-6 subunit × 2 (Q8IK90) 20S proteasome alpha-7 subunit × 2 (O77396) 20S proteasome beta-1 subunit × 2 (Q8I0U7) 20S proteasome beta-3 subunit × 2 (Q8I261) 20S proteasome beta-4 subunit × 2 (Q8IKC9) 20S proteasome beta-5 subunit × 2 (Q8IJT1) 20S proteasome beta-6 subunit × 2 (C0H4E8) 20S proteasome beta-7 subunit × 2 (Q7K6A9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;wait time 0sec blot time 2sec blot force -1 Resolution 3.60 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

20S proteasome beta-3 subunit

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 20S proteasome alpha-1 subunit × 2 (Q8IAR3) 20S proteasome alpha-2 subunit × 2 (C6KST3) 20S proteasome alpha-3 subunit × 2 (Q8IDG3) 20S proteasome alpha-4 subunit × 2 (Q8IDG2) 20S proteasome alpha-5 subunit × 2 (Q8IBI3) 20S proteasome alpha-6 subunit × 2 (Q8IK90) 20S proteasome alpha-7 subunit × 2 (O77396) 20S proteasome beta-1 subunit × 2 (Q8I0U7) 20S proteasome beta-2 subunit × 2 (Q8I6T3) 20S proteasome beta-4 subunit × 2 (Q8IKC9) 20S proteasome beta-5 subunit × 2 (Q8IJT1) 20S proteasome beta-6 subunit × 2 (C0H4E8) 20S proteasome beta-7 subunit × 2 (Q7K6A9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;wait time 0sec blot time 2sec blot force -1 Resolution 3.60 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

20S proteasome beta-4 subunit

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 20S proteasome alpha-1 subunit × 2 (Q8IAR3) 20S proteasome alpha-2 subunit × 2 (C6KST3) 20S proteasome alpha-3 subunit × 2 (Q8IDG3) 20S proteasome alpha-4 subunit × 2 (Q8IDG2) 20S proteasome alpha-5 subunit × 2 (Q8IBI3) 20S proteasome alpha-6 subunit × 2 (Q8IK90) 20S proteasome alpha-7 subunit × 2 (O77396) 20S proteasome beta-1 subunit × 2 (Q8I0U7) 20S proteasome beta-2 subunit × 2 (Q8I6T3) 20S proteasome beta-3 subunit × 2 (Q8I261) 20S proteasome beta-5 subunit × 2 (Q8IJT1) 20S proteasome beta-6 subunit × 2 (C0H4E8) 20S proteasome beta-7 subunit × 2 (Q7K6A9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;wait time 0sec blot time 2sec blot force -1 Resolution 3.60 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

20S proteasome beta-5 subunit

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 20S proteasome alpha-1 subunit × 2 (Q8IAR3) 20S proteasome alpha-2 subunit × 2 (C6KST3) 20S proteasome alpha-3 subunit × 2 (Q8IDG3) 20S proteasome alpha-4 subunit × 2 (Q8IDG2) 20S proteasome alpha-5 subunit × 2 (Q8IBI3) 20S proteasome alpha-6 subunit × 2 (Q8IK90) 20S proteasome alpha-7 subunit × 2 (O77396) 20S proteasome beta-1 subunit × 2 (Q8I0U7) 20S proteasome beta-2 subunit × 2 (Q8I6T3) 20S proteasome beta-3 subunit × 2 (Q8I261) 20S proteasome beta-4 subunit × 2 (Q8IKC9) 20S proteasome beta-6 subunit × 2 (C0H4E8) 20S proteasome beta-7 subunit × 2 (Q7K6A9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;wait time 0sec blot time 2sec blot force -1 Resolution 3.60 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

20S proteasome beta-6 subunit

OrganismNot specified

UniProt C0H4E8

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 20S proteasome alpha-1 subunit × 2 (Q8IAR3) 20S proteasome alpha-2 subunit × 2 (C6KST3) 20S proteasome alpha-3 subunit × 2 (Q8IDG3) 20S proteasome alpha-4 subunit × 2 (Q8IDG2) 20S proteasome alpha-5 subunit × 2 (Q8IBI3) 20S proteasome alpha-6 subunit × 2 (Q8IK90) 20S proteasome alpha-7 subunit × 2 (O77396) 20S proteasome beta-1 subunit × 2 (Q8I0U7) 20S proteasome beta-2 subunit × 2 (Q8I6T3) 20S proteasome beta-3 subunit × 2 (Q8I261) 20S proteasome beta-4 subunit × 2 (Q8IKC9) 20S proteasome beta-5 subunit × 2 (Q8IJT1) 20S proteasome beta-7 subunit × 2 (Q7K6A9) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;wait time 0sec blot time 2sec blot force -1 Resolution 3.60 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 C0H4E8_PLAF7
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

20S proteasome beta-7 subunit

OrganismNot specified

UniProt Q7K6A9

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 20S proteasome alpha-1 subunit × 2 (Q8IAR3) 20S proteasome alpha-2 subunit × 2 (C6KST3) 20S proteasome alpha-3 subunit × 2 (Q8IDG3) 20S proteasome alpha-4 subunit × 2 (Q8IDG2) 20S proteasome alpha-5 subunit × 2 (Q8IBI3) 20S proteasome alpha-6 subunit × 2 (Q8IK90) 20S proteasome alpha-7 subunit × 2 (O77396) 20S proteasome beta-1 subunit × 2 (Q8I0U7) 20S proteasome beta-2 subunit × 2 (Q8I6T3) 20S proteasome beta-3 subunit × 2 (Q8I261) 20S proteasome beta-4 subunit × 2 (Q8IKC9) 20S proteasome beta-5 subunit × 2 (Q8IJT1) 20S proteasome beta-6 subunit × 2 (C0H4E8) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE;wait time 0sec blot time 2sec blot force -1 Resolution 3.60 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.

7 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q7K6A9_PLAF7
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 6muw

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6muw
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6muw
Deposition date deposition_date2018-10-23
Structure title titleThe structure of the Plasmodium falciparum 20S proteasome.
Keywords keywordsproteasome, protease, HYDROLASE; HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.24
Radius of gyration Rg (electron density) rg_electron59.88
Forward intensity I(0) i06785460000.00
Molecular weight molecular_weight708100.0 kDa
Excluded volume excluded_volume890740 ų
Envelope volume envelope_volume1287700 ų
Hydration-shell volume shell_volume171370 ų
Envelope diameter envelope_diameter194.3
Shell Rg shell_rg68.39
Envelope Rg envelope_rg58.06
Shape Rg shape_rg59.85
Total Rg total_rg60.16
Total atoms total_atoms49798
Residues n_residues6252
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 dmax173.1
Rg (real space) rg_real59.95
Rg uncertainty (real space) rg_real_error1.05
I(0) (real space) i0_real6.7850e+09
I(0) uncertainty (real space) i0_real_error1.3100e+08
Rg (reciprocal space) rg_reciprocal60.47
I(0) (reciprocal space) i0_reciprocal6791000000.0000
Solution quality estimate total_estimate0.8358
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary79.9
Skewness Skewness skewness0.198
Kurtosis Kurtosis kurtosis-0.437
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha985900000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.956; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.004

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (14)

7. Fold Classification (SCOP + CATH) 28 domains

CATH v4.4 (28 domains)

Domain ID domain_id6muwA00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwB00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwC00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwD00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwE00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwF00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwG00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwH00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwI00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwJ00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwK00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwL00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwM00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwN00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwO00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwP00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwQ00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwR00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwS00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwT00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwU00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwV00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwW00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwX00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwY00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwZ00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwa00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain
Domain ID domain_id6muwb00
Class class3 — Alpha Beta
Architecture architecture60 — 4-Layer Sandwich
Topology topology20 — Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Homologous superfamily homologous superfamily10 — Aminohydrolase, N-terminal nucleophile (Ntn) domain

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9. Files and Curves (10)