9eg8

Cryo-EM structure of COP9 signalosome precatalytic state with neddylated cullin-4A

Method: ELECTRON MICROSCOPY Dmax: 184.8 Å Quality: REASONABLE

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain E; UniProt 1–334 Mutation:E76A, D151N NEDD8 × 1 (Q15843) Cullin-4A × 1 (Q13619) 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) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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

NEDD8

Homo sapiens

UniProt Q15843

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain I; UniProt 1–81 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) Cullin-4A × 1 (Q13619) 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) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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.

46 other PDB entries and 71 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name NEDD8_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain I; PDBConstruct 1–81; UniProt 1–81

Cullin-4A

Homo sapiens

UniProt Q13619

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain J; UniProt 1–759 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) NEDD8 × 1 (Q15843) 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) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL4A_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain J; PDBConstruct 1–759; UniProt 1–759

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain A; UniProt 1–491 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) NEDD8 × 1 (Q15843) Cullin-4A × 1 (Q13619) 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) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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 4
Chains and sequence ranges Author chain A; PDBConstruct 1–491; UniProt 1–491

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain B; UniProt 1–443 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) NEDD8 × 1 (Q15843) Cullin-4A × 1 (Q13619) 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) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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 5
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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain C; UniProt 1–423 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) NEDD8 × 1 (Q15843) Cullin-4A × 1 (Q13619) 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) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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 6
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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain D; UniProt 1–406 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) NEDD8 × 1 (Q15843) Cullin-4A × 1 (Q13619) 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) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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 7
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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain F; UniProt 1–327 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) NEDD8 × 1 (Q15843) Cullin-4A × 1 (Q13619) 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) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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 8
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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain G; UniProt 1–264 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) NEDD8 × 1 (Q15843) Cullin-4A × 1 (Q13619) 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) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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 9
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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain H; UniProt 1–209 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) NEDD8 × 1 (Q15843) Cullin-4A × 1 (Q13619) 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) E3 ubiquitin-protein ligase RBX1 × 1 (P62877) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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 10
Chains and sequence ranges Author chain H; PDBConstruct 1–209; UniProt 1–209

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 × 11 PDB declaration: undecameric(11) Consistent with protein copy count Chain K; UniProt 1–108 Not recorded COP9 signalosome complex subunit 5 × 1 (Q92905) NEDD8 × 1 (Q15843) Cullin-4A × 1 (Q13619) 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) ZN ZINC ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.39 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 K; 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 9eg8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9eg8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9eg8
Deposition date deposition_date2024-11-21
Structure title titleCryo-EM structure of COP9 signalosome precatalytic state with neddylated cullin-4A
Keywords keywordsCOP9, COP9 signalosome, signalosome, deneddylation, CSN5, metalloprotease, N8CUL4A, CUL4A, deneddylation complex, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.62
Radius of gyration Rg (electron density) rg_electron55.66
Forward intensity I(0) i01730760000.00
Molecular weight molecular_weight352320.0 kDa
Excluded volume excluded_volume443170 ų
Envelope volume envelope_volume691420 ų
Hydration-shell volume shell_volume104360 ų
Envelope diameter envelope_diameter198.8
Shell Rg shell_rg58.16
Envelope Rg envelope_rg54.02
Shape Rg shape_rg55.66
Total Rg total_rg55.71
Total atoms total_atoms24745
Residues n_residues3082
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 dmax184.8
Rg (real space) rg_real55.54
Rg uncertainty (real space) rg_real_error1.89
I(0) (real space) i0_real1.7310e+09
I(0) uncertainty (real space) i0_real_error3.4510e+07
Rg (reciprocal space) rg_reciprocal55.68
I(0) (reciprocal space) i0_reciprocal1731000000.0000
Solution quality estimate total_estimate0.6496
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary66.0
Skewness Skewness skewness0.302
Kurtosis Kurtosis kurtosis-0.157
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha109100000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.860; Stabil: 1.000; Sysdev: 0.041; Positv: 1.000; Valcen: 0.988; Smooth: 0.750

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)