7q40

Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2

Method: X-RAY DIFFRACTION Dmax: 103.8 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 2938–3342 Not recorded CIT CITRIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293.15 K;hanging drop 20% PEG 3350 0.18M tris amonium citrate Resolution 2.35 Å R-free 0.230
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 2938–3342 Not recorded CIT CITRIC ACID × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293.15 K;hanging drop 20% PEG 3350 0.18M tris amonium citrate Resolution 2.35 Å R-free 0.230
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain E; UniProt 2938–3342 Not recorded CIT CITRIC ACID × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293.15 K;hanging drop 20% PEG 3350 0.18M tris amonium citrate Resolution 2.35 Å R-free 0.230

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 31 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 1–405; UniProt 2938–3342 Author chain C; PDBConstruct 1–405; UniProt 2938–3342 Author chain E; PDBConstruct 1–405; UniProt 2938–3342

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 7q40

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7q40
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7q40
Deposition date deposition_date2021-10-29
Structure title titleCrystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2
Keywords keywords7-bladed beta-propeller HERC2 RCC1-like Domain 2 RLD2 ubiquitin ligase DXDKDED motif, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier34.19
Radius of gyration Rg (electron density) rg_electron33.93
Forward intensity I(0) i0230437000.00
Molecular weight molecular_weight119020.0 kDa
Excluded volume excluded_volume147780 ų
Envelope volume envelope_volume178630 ų
Hydration-shell volume shell_volume43423 ų
Envelope diameter envelope_diameter107.5
Shell Rg shell_rg40.72
Envelope Rg envelope_rg33.78
Shape Rg shape_rg33.89
Total Rg total_rg34.51
Total atoms total_atoms8411
Residues n_residues1108
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 dmax103.8
Rg (real space) rg_real34.09
Rg uncertainty (real space) rg_real_error0.65
I(0) (real space) i0_real2.3040e+08
I(0) uncertainty (real space) i0_real_error3.3780e+06
Rg (reciprocal space) rg_reciprocal34.15
I(0) (reciprocal space) i0_reciprocal230400000.0000
Solution quality estimate total_estimate0.9016
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary33.9
Skewness Skewness skewness0.129
Kurtosis Kurtosis kurtosis-0.758
Angular range angular_range— – 0.2300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha55640000.0000
Real-space data points n_real_points47
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.966; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.818

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)