9t7v

Structure of LRRC58-EloB/C-CDO1 in complex with NEDD8-CUL5-RBX2-ARIH2-Ub

Method: ELECTRON MICROSCOPY Dmax: 201.8 Å Quality: GOOD

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

Cysteine dioxygenase type 1

Homo sapiens

UniProt Q16878

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 1–200 Mutation:K8C, C76A, C93S, C130A, C164S RING-box protein 2 × 1 (Q9UBF6) Ubiquitin × 1 (P0CG48) Elongin-C × 1 (Q15369) NEDD8 × 1 (Q15843) Cullin-5 × 1 (Q93034) E3 ubiquitin-protein ligase ARIH2 × 1 (O95376) Elongin-B × 1 (Q15370) Leucine-rich repeat-containing protein 58 × 1 (Q96CX6) FE FE (III) ION × 1 SY8 5-azanylpentan-2-one × 1 ZN ZINC ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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.

17 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CDO1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–200; UniProt 1–200

RING-box protein 2

Homo sapiens

UniProt Q9UBF6

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain R; UniProt 5–113 Mutation:N-terminal residues 1-4 deleted Cysteine dioxygenase type 1 × 1 (Q16878) Ubiquitin × 1 (P0CG48) Elongin-C × 1 (Q15369) NEDD8 × 1 (Q15843) Cullin-5 × 1 (Q93034) E3 ubiquitin-protein ligase ARIH2 × 1 (O95376) Elongin-B × 1 (Q15370) Leucine-rich repeat-containing protein 58 × 1 (Q96CX6) FE FE (III) ION × 1 SY8 5-azanylpentan-2-one × 1 ZN ZINC ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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.

6 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RBX2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain R; PDBConstruct 1–109; UniProt 5–113

Ubiquitin

Homo sapiens

UniProt P0CG48

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain U; UniProt 1–75 Not recorded Cysteine dioxygenase type 1 × 1 (Q16878) RING-box protein 2 × 1 (Q9UBF6) Elongin-C × 1 (Q15369) NEDD8 × 1 (Q15843) Cullin-5 × 1 (Q93034) E3 ubiquitin-protein ligase ARIH2 × 1 (O95376) Elongin-B × 1 (Q15370) Leucine-rich repeat-containing protein 58 × 1 (Q96CX6) FE FE (III) ION × 1 SY8 5-azanylpentan-2-one × 1 ZN ZINC ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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.

219 other PDB entries and 348 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBC_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain U; PDBConstruct 1–75; UniProt 1–75

Elongin-C

Homo sapiens

UniProt Q15369

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain O; UniProt 1–112 Not recorded Cysteine dioxygenase type 1 × 1 (Q16878) RING-box protein 2 × 1 (Q9UBF6) Ubiquitin × 1 (P0CG48) NEDD8 × 1 (Q15843) Cullin-5 × 1 (Q93034) E3 ubiquitin-protein ligase ARIH2 × 1 (O95376) Elongin-B × 1 (Q15370) Leucine-rich repeat-containing protein 58 × 1 (Q96CX6) FE FE (III) ION × 1 SY8 5-azanylpentan-2-one × 1 ZN ZINC ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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.

220 other PDB entries and 467 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOC_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain O; PDBConstruct 1–112; UniProt 1–112

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain N; UniProt 1–76 Not recorded Cysteine dioxygenase type 1 × 1 (Q16878) RING-box protein 2 × 1 (Q9UBF6) Ubiquitin × 1 (P0CG48) Elongin-C × 1 (Q15369) Cullin-5 × 1 (Q93034) E3 ubiquitin-protein ligase ARIH2 × 1 (O95376) Elongin-B × 1 (Q15370) Leucine-rich repeat-containing protein 58 × 1 (Q96CX6) FE FE (III) ION × 1 SY8 5-azanylpentan-2-one × 1 ZN ZINC ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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 5
Chains and sequence ranges Author chain N; PDBConstruct 1–76; UniProt 1–76

Cullin-5

Homo sapiens

UniProt Q93034

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain C; UniProt 1–780 Not recorded Cysteine dioxygenase type 1 × 1 (Q16878) RING-box protein 2 × 1 (Q9UBF6) Ubiquitin × 1 (P0CG48) Elongin-C × 1 (Q15369) NEDD8 × 1 (Q15843) E3 ubiquitin-protein ligase ARIH2 × 1 (O95376) Elongin-B × 1 (Q15370) Leucine-rich repeat-containing protein 58 × 1 (Q96CX6) FE FE (III) ION × 1 SY8 5-azanylpentan-2-one × 1 ZN ZINC ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CUL5_HUMAN
Isoform
PDB entities 6
Chains and sequence ranges Author chain C; PDBConstruct 1–780; UniProt 1–780

E3 ubiquitin-protein ligase ARIH2

Homo sapiens

UniProt O95376

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain H; UniProt 1–493 Mutation:L381A,E382A,E455A, Cysteine dioxygenase type 1 × 1 (Q16878) RING-box protein 2 × 1 (Q9UBF6) Ubiquitin × 1 (P0CG48) Elongin-C × 1 (Q15369) NEDD8 × 1 (Q15843) Cullin-5 × 1 (Q93034) Elongin-B × 1 (Q15370) Leucine-rich repeat-containing protein 58 × 1 (Q96CX6) FE FE (III) ION × 1 SY8 5-azanylpentan-2-one × 1 ZN ZINC ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ARI2_HUMAN
Isoform
PDB entities 7
Chains and sequence ranges Author chain H; PDBConstruct 1–493; UniProt 1–493

Elongin-B

Homo sapiens

UniProt Q15370

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain I; UniProt 1–118 Not recorded Cysteine dioxygenase type 1 × 1 (Q16878) RING-box protein 2 × 1 (Q9UBF6) Ubiquitin × 1 (P0CG48) Elongin-C × 1 (Q15369) NEDD8 × 1 (Q15843) Cullin-5 × 1 (Q93034) E3 ubiquitin-protein ligase ARIH2 × 1 (O95376) Leucine-rich repeat-containing protein 58 × 1 (Q96CX6) FE FE (III) ION × 1 SY8 5-azanylpentan-2-one × 1 ZN ZINC ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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.

228 other PDB entries and 478 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ELOB_HUMAN
Isoform
PDB entities 8
Chains and sequence ranges Author chain I; PDBConstruct 1–118; UniProt 1–118

Leucine-rich repeat-containing protein 58

Homo sapiens

UniProt Q96CX6

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 × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain B; UniProt 1–371 Not recorded Cysteine dioxygenase type 1 × 1 (Q16878) RING-box protein 2 × 1 (Q9UBF6) Ubiquitin × 1 (P0CG48) Elongin-C × 1 (Q15369) NEDD8 × 1 (Q15843) Cullin-5 × 1 (Q93034) E3 ubiquitin-protein ligase ARIH2 × 1 (O95376) Elongin-B × 1 (Q15370) FE FE (III) ION × 1 SY8 5-azanylpentan-2-one × 1 ZN ZINC ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.95 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 LRC58_HUMAN
Isoform
PDB entities 9
Chains and sequence ranges Author chain B; PDBConstruct 1–371; UniProt 1–371

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 9t7v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9t7v
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9t7v
Deposition date deposition_date2025-11-12
Structure title titleStructure of LRRC58-EloB/C-CDO1 in complex with NEDD8-CUL5-RBX2-ARIH2-Ub
Keywords keywordsCullin, E3 ligase, Ubiquitin, LIGASE; LIGASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier58.06
Radius of gyration Rg (electron density) rg_electron58.48
Forward intensity I(0) i0662957000.00
Molecular weight molecular_weight214530.0 kDa
Excluded volume excluded_volume268180 ų
Envelope volume envelope_volume473840 ų
Hydration-shell volume shell_volume69396 ų
Envelope diameter envelope_diameter199.0
Shell Rg shell_rg60.32
Envelope Rg envelope_rg55.54
Shape Rg shape_rg58.54
Total Rg total_rg58.33
Total atoms total_atoms15047
Residues n_residues1893
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 dmax201.8
Rg (real space) rg_real58.23
Rg uncertainty (real space) rg_real_error2.85
I(0) (real space) i0_real6.6300e+08
I(0) uncertainty (real space) i0_real_error1.4020e+07
Rg (reciprocal space) rg_reciprocal57.89
I(0) (reciprocal space) i0_reciprocal662600000.0000
Solution quality estimate total_estimate0.8585
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary74.8
Skewness Skewness skewness0.295
Kurtosis Kurtosis kurtosis-0.437
Angular range angular_range— – 0.1350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26530000.0000
Real-space data points n_real_points28
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.872; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.929; Smooth: 0.610

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (12)

8. Citations (1)

9. Files and Curves (10)