8h3a

Cryo-EM Structure of the KBTBD2-CRL3~N8(removed)-CSN complex

Method: ELECTRON MICROSCOPY Dmax: 211.0 Å Quality: GOOD

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

COP9 signalosome complex subunit 5

Homo sapiens

UniProt Q92905

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain E; UniProt 1–334 Not recorded COP9 signalosome complex subunit 1 × 1 (Q13098) COP9 signalosome complex subunit 2 × 1 (P61201) COP9 signalosome complex subunit 3 × 1 (Q9UNS2) COP9 signalosome complex subunit 4 × 1 (Q9BT78) COP9 signalosome complex subunit 6 × 1 (Q7L5N1) COP9 signalosome complex subunit 7b × 1 (Q9H9Q2) COP9 signalosome complex subunit 8 × 1 (Q99627) Kelch repeat and BTB domain-containing protein 2 × 2 (Q8IY47) Cullin-3 × 1 (Q13618) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.51 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.

30 other PDB entries and 38 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSN5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–334; UniProt 1–334

COP9 signalosome complex subunit 1

Homo sapiens

UniProt Q13098

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 12–491 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) COP9 signalosome complex subunit 2 × 1 (P61201) COP9 signalosome complex subunit 3 × 1 (Q9UNS2) COP9 signalosome complex subunit 4 × 1 (Q9BT78) COP9 signalosome complex subunit 6 × 1 (Q7L5N1) COP9 signalosome complex subunit 7b × 1 (Q9H9Q2) COP9 signalosome complex subunit 8 × 1 (Q99627) Kelch repeat and BTB domain-containing protein 2 × 2 (Q8IY47) Cullin-3 × 1 (Q13618) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.51 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.

27 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSN1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 52–527; UniProt 12–491

COP9 signalosome complex subunit 2

Homo sapiens

UniProt P61201

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain B; UniProt 1–443 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) COP9 signalosome complex subunit 1 × 1 (Q13098) COP9 signalosome complex subunit 3 × 1 (Q9UNS2) COP9 signalosome complex subunit 4 × 1 (Q9BT78) COP9 signalosome complex subunit 6 × 1 (Q7L5N1) COP9 signalosome complex subunit 7b × 1 (Q9H9Q2) COP9 signalosome complex subunit 8 × 1 (Q99627) Kelch repeat and BTB domain-containing protein 2 × 2 (Q8IY47) Cullin-3 × 1 (Q13618) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.51 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.

28 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSN2_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain B; PDBConstruct 1–443; UniProt 1–443

COP9 signalosome complex subunit 3

Homo sapiens

UniProt Q9UNS2

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain C; UniProt 1–423 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) COP9 signalosome complex subunit 1 × 1 (Q13098) COP9 signalosome complex subunit 2 × 1 (P61201) COP9 signalosome complex subunit 4 × 1 (Q9BT78) COP9 signalosome complex subunit 6 × 1 (Q7L5N1) COP9 signalosome complex subunit 7b × 1 (Q9H9Q2) COP9 signalosome complex subunit 8 × 1 (Q99627) Kelch repeat and BTB domain-containing protein 2 × 2 (Q8IY47) Cullin-3 × 1 (Q13618) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.51 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.

27 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSN3_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain C; PDBConstruct 1–423; UniProt 1–423

COP9 signalosome complex subunit 4

Homo sapiens

UniProt Q9BT78

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain D; UniProt 1–406 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) COP9 signalosome complex subunit 1 × 1 (Q13098) COP9 signalosome complex subunit 2 × 1 (P61201) COP9 signalosome complex subunit 3 × 1 (Q9UNS2) COP9 signalosome complex subunit 6 × 1 (Q7L5N1) COP9 signalosome complex subunit 7b × 1 (Q9H9Q2) COP9 signalosome complex subunit 8 × 1 (Q99627) Kelch repeat and BTB domain-containing protein 2 × 2 (Q8IY47) Cullin-3 × 1 (Q13618) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.51 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.

28 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSN4_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain D; PDBConstruct 1–406; UniProt 1–406

COP9 signalosome complex subunit 6

Homo sapiens

UniProt Q7L5N1

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain F; UniProt 1–327 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) COP9 signalosome complex subunit 1 × 1 (Q13098) COP9 signalosome complex subunit 2 × 1 (P61201) COP9 signalosome complex subunit 3 × 1 (Q9UNS2) COP9 signalosome complex subunit 4 × 1 (Q9BT78) COP9 signalosome complex subunit 7b × 1 (Q9H9Q2) COP9 signalosome complex subunit 8 × 1 (Q99627) Kelch repeat and BTB domain-containing protein 2 × 2 (Q8IY47) Cullin-3 × 1 (Q13618) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.51 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.

28 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSN6_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain F; PDBConstruct 1–327; UniProt 1–327

COP9 signalosome complex subunit 7b

Homo sapiens

UniProt Q9H9Q2

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain G; UniProt 1–264 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) COP9 signalosome complex subunit 1 × 1 (Q13098) COP9 signalosome complex subunit 2 × 1 (P61201) COP9 signalosome complex subunit 3 × 1 (Q9UNS2) COP9 signalosome complex subunit 4 × 1 (Q9BT78) COP9 signalosome complex subunit 6 × 1 (Q7L5N1) COP9 signalosome complex subunit 8 × 1 (Q99627) Kelch repeat and BTB domain-containing protein 2 × 2 (Q8IY47) Cullin-3 × 1 (Q13618) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.51 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.

23 other PDB entries and 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSN7B_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain G; PDBConstruct 1–264; UniProt 1–264

COP9 signalosome complex subunit 8

Homo sapiens

UniProt Q99627

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain H; UniProt 1–209 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) COP9 signalosome complex subunit 1 × 1 (Q13098) COP9 signalosome complex subunit 2 × 1 (P61201) COP9 signalosome complex subunit 3 × 1 (Q9UNS2) COP9 signalosome complex subunit 4 × 1 (Q9BT78) COP9 signalosome complex subunit 6 × 1 (Q7L5N1) COP9 signalosome complex subunit 7b × 1 (Q9H9Q2) Kelch repeat and BTB domain-containing protein 2 × 2 (Q8IY47) Cullin-3 × 1 (Q13618) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.51 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.

27 other PDB entries and 34 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CSN8_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain H; PDBConstruct 1–209; UniProt 1–209

Kelch repeat and BTB domain-containing protein 2

Homo sapiens

UniProt Q8IY47

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain I; UniProt 1–623 Chain M; UniProt 1–623 Mutation:S252D COP9 signalosome complex subunit 5 × 1 (Q92905) COP9 signalosome complex subunit 1 × 1 (Q13098) COP9 signalosome complex subunit 2 × 1 (P61201) COP9 signalosome complex subunit 3 × 1 (Q9UNS2) COP9 signalosome complex subunit 4 × 1 (Q9BT78) COP9 signalosome complex subunit 6 × 1 (Q7L5N1) COP9 signalosome complex subunit 7b × 1 (Q9H9Q2) COP9 signalosome complex subunit 8 × 1 (Q99627) Cullin-3 × 1 (Q13618) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.51 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 KBTB2_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain I; PDBConstruct 1–623; UniProt 1–623 Author chain M; PDBConstruct 1–623; UniProt 1–623

Cullin-3

Homo sapiens

UniProt Q13618

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain L; UniProt 1–768 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) COP9 signalosome complex subunit 1 × 1 (Q13098) COP9 signalosome complex subunit 2 × 1 (P61201) COP9 signalosome complex subunit 3 × 1 (Q9UNS2) COP9 signalosome complex subunit 4 × 1 (Q9BT78) COP9 signalosome complex subunit 6 × 1 (Q7L5N1) COP9 signalosome complex subunit 7b × 1 (Q9H9Q2) COP9 signalosome complex subunit 8 × 1 (Q99627) Kelch repeat and BTB domain-containing protein 2 × 2 (Q8IY47) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.51 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.

29 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL3_HUMAN
Isoform
PDB entities 10
Chains and sequence ranges Author chain L; PDBConstruct 1–768; UniProt 1–768

E3 ubiquitin-protein ligase RBX1

Homo sapiens

UniProt P62877

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain R; UniProt 1–108 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) COP9 signalosome complex subunit 1 × 1 (Q13098) COP9 signalosome complex subunit 2 × 1 (P61201) COP9 signalosome complex subunit 3 × 1 (Q9UNS2) COP9 signalosome complex subunit 4 × 1 (Q9BT78) COP9 signalosome complex subunit 6 × 1 (Q7L5N1) COP9 signalosome complex subunit 7b × 1 (Q9H9Q2) COP9 signalosome complex subunit 8 × 1 (Q99627) Kelch repeat and BTB domain-containing protein 2 × 2 (Q8IY47) Cullin-3 × 1 (Q13618) ZN ZINC ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.51 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.

99 other PDB entries and 107 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBX1_HUMAN
Isoform
PDB entities 11
Chains and sequence ranges Author chain R; PDBConstruct 1–108; UniProt 1–108

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 8h3a

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8h3a
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8h3a
Deposition date deposition_date2022-10-08
Structure title titleCryo-EM Structure of the KBTBD2-CRL3~N8(removed)-CSN complex
Keywords keywordsligase, complex; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier63.99
Radius of gyration Rg (electron density) rg_electron63.65
Forward intensity I(0) i03800790000.00
Molecular weight molecular_weight522860.0 kDa
Excluded volume excluded_volume655540 ų
Envelope volume envelope_volume1065500 ų
Hydration-shell volume shell_volume138470 ų
Envelope diameter envelope_diameter205.9
Shell Rg shell_rg67.08
Envelope Rg envelope_rg60.72
Shape Rg shape_rg63.66
Total Rg total_rg63.68
Total atoms total_atoms36704
Residues n_residues4560
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 dmax211.0
Rg (real space) rg_real63.63
Rg uncertainty (real space) rg_real_error1.75
I(0) (real space) i0_real3.8010e+09
I(0) uncertainty (real space) i0_real_error7.4440e+07
Rg (reciprocal space) rg_reciprocal64.26
I(0) (reciprocal space) i0_reciprocal3805000000.0000
Solution quality estimate total_estimate0.8798
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary84.4
Skewness Skewness skewness0.115
Kurtosis Kurtosis kurtosis-0.508
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha208700000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.883; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.825

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)