7q46

Crystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2 in complex with DXDKDED motif of pericentriolar material 1 protein

Method: X-RAY DIFFRACTION Dmax: 103.6 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 2941–3342 Not recorded Pericentriolar material 1 protein × 1 (Q15154) 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 2.46 Å R-free 0.245
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 2941–3342 Not recorded Pericentriolar material 1 protein × 1 (Q15154) 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 2.46 Å R-free 0.245
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 2941–3342 Not recorded Pericentriolar material 1 protein × 1 (Q15154) CIT CITRIC ACID × 1 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 2.46 Å R-free 0.245

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 4–405; UniProt 2941–3342 Author chain C; PDBConstruct 4–405; UniProt 2941–3342 Author chain E; PDBConstruct 4–405; UniProt 2941–3342

Pericentriolar material 1 protein

OrganismNot specified

UniProt Q15154

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 B; UniProt 1737–1751 Not recorded E3 ubiquitin-protein ligase HERC2 × 1 (O95714) 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 2.46 Å R-free 0.245
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1737–1751 Not recorded E3 ubiquitin-protein ligase HERC2 × 1 (O95714) 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 2.46 Å R-free 0.245
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 1737–1751 Not recorded E3 ubiquitin-protein ligase HERC2 × 1 (O95714) CIT CITRIC ACID × 1 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 2.46 Å R-free 0.245

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.

2 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PCM1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–15; UniProt 1737–1751 Author chain D; PDBConstruct 1–15; UniProt 1737–1751 Author chain F; PDBConstruct 1–15; UniProt 1737–1751

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 7q46

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7q46
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7q46
Deposition date deposition_date2021-10-29
Structure title titleCrystal structure of RCC1-Like domain 2 of ubiquitin ligase HERC2 in complex with DXDKDED motif of pericentriolar material 1 protein
Keywords keywords;7-bladed beta-propeller HERC2 RCC1-like Domain 2 RLD2 ubiquitin ligase PCM1 pericentriolar material 1 protein 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_guinier33.93
Radius of gyration Rg (electron density) rg_electron33.70
Forward intensity I(0) i0233119000.00
Molecular weight molecular_weight119770.0 kDa
Excluded volume excluded_volume148760 ų
Envelope volume envelope_volume178620 ų
Hydration-shell volume shell_volume43688 ų
Envelope diameter envelope_diameter106.8
Shell Rg shell_rg40.49
Envelope Rg envelope_rg33.55
Shape Rg shape_rg33.66
Total Rg total_rg34.28
Total atoms total_atoms8427
Residues n_residues1128
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 dmax103.6
Rg (real space) rg_real33.84
Rg uncertainty (real space) rg_real_error0.62
I(0) (real space) i0_real2.3310e+08
I(0) uncertainty (real space) i0_real_error3.5790e+06
Rg (reciprocal space) rg_reciprocal33.90
I(0) (reciprocal space) i0_reciprocal233100000.0000
Solution quality estimate total_estimate0.9045
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary35.3
Skewness Skewness skewness0.131
Kurtosis Kurtosis kurtosis-0.750
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha60540000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.962; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.872

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)