9l93

Crystal structure of NCOA4 in complex with HERC2

Method: X-RAY DIFFRACTION Dmax: 87.7 Å Quality: EXCELLENT

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

E3 ubiquitin-protein ligase HERC2

Homo sapiens

UniProt O95714

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 2539–2700 Not recorded Nuclear receptor coactivator 4 × 1 (Q13772) FES FE2/S2 (INORGANIC) CLUSTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;289 K;18% v/v 2-Propanol, 0.1 M Sodium citrate tribasic dihydrate (pH 5.5), 20% w/v Polyethylene glycol 4000 Resolution 1.73 Å R-free 0.207
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 2539–2700 Not recorded Nuclear receptor coactivator 4 × 1 (Q13772) FES FE2/S2 (INORGANIC) CLUSTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;289 K;18% v/v 2-Propanol, 0.1 M Sodium citrate tribasic dihydrate (pH 5.5), 20% w/v Polyethylene glycol 4000 Resolution 1.73 Å R-free 0.207

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.

14 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name HERC2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–164; UniProt 2539–2700 Author chain B; PDBConstruct 3–164; UniProt 2539–2700

Nuclear receptor coactivator 4

Homo sapiens

UniProt Q13772

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 395–442 Not recorded E3 ubiquitin-protein ligase HERC2 × 1 (O95714) FES FE2/S2 (INORGANIC) CLUSTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;289 K;18% v/v 2-Propanol, 0.1 M Sodium citrate tribasic dihydrate (pH 5.5), 20% w/v Polyethylene glycol 4000 Resolution 1.73 Å R-free 0.207
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 395–442 Not recorded E3 ubiquitin-protein ligase HERC2 × 1 (O95714) FES FE2/S2 (INORGANIC) CLUSTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;289 K;18% v/v 2-Propanol, 0.1 M Sodium citrate tribasic dihydrate (pH 5.5), 20% w/v Polyethylene glycol 4000 Resolution 1.73 Å R-free 0.207

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 NCOA4_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 4–51; UniProt 395–442 Author chain D; PDBConstruct 4–51; UniProt 395–442

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 9l93

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9l93
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9l93
Deposition date deposition_date2024-12-29
最后修订 last_revision2025-11-05
Structure title titleCrystal structure of NCOA4 in complex with HERC2
Keywords keywordsNCOA4, HERC2, Iron-Sulfur Cluster, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.99
Radius of gyration Rg (electron density) rg_electron26.58
Forward intensity I(0) i036655300.00
Molecular weight molecular_weight45335.0 kDa
Excluded volume excluded_volume56134 ų
Envelope volume envelope_volume73551 ų
Hydration-shell volume shell_volume24196 ų
Envelope diameter envelope_diameter92.1
Shell Rg shell_rg32.56
Envelope Rg envelope_rg26.07
Shape Rg shape_rg26.63
Total Rg total_rg27.10
Total atoms total_atoms3158
Residues n_residues396
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 dmax87.7
Rg (real space) rg_real26.99
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real3.6660e+07
I(0) uncertainty (real space) i0_real_error5.0470e+05
Rg (reciprocal space) rg_reciprocal26.99
I(0) (reciprocal space) i0_reciprocal36660000.0000
Solution quality estimate total_estimate0.9051
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary32.7
Skewness Skewness skewness0.281
Kurtosis Kurtosis kurtosis-0.470
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3298000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.940; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.951; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)