8w31

Crystal structure of parkin (R0RB):2pUb with activator compound

Method: X-RAY DIFFRACTION Dmax: 91.5 Å Quality: REASONABLE

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

E3 ubiquitin-protein ligase parkin

Rattus norvegicus

UniProt Q9JK66

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 145–379 Fragment:residues 145-379 Ubiquitin × 2 (P0CG47) ZN ZINC ION × 6 A1AE9 (S)-1-(6-benzyl-3-(4-(1,2,3,4-tetrahydroquinoline-1-carbonyl)phenyl)-6,7-dihydropyrazolo[1,5-a]pyrazin-5(4H)-yl)ethan-1-one × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;277 K;0.2 M Sodium Chloride, 0.1M HEPES pH 7.5, 25% (w/v) PEG 3350 Resolution 2.50 Å R-free 0.294

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 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRKN_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–240; UniProt 145–379

Ubiquitin

Homo sapiens

UniProt P0CG47

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–75 Chain C; UniProt 1–75 Fragment:residues 1-75 Non-standard monomer:Yes (specific site not provided by mmCIF) E3 ubiquitin-protein ligase parkin × 1 (Q9JK66) ZN ZINC ION × 6 A1AE9 (S)-1-(6-benzyl-3-(4-(1,2,3,4-tetrahydroquinoline-1-carbonyl)phenyl)-6,7-dihydropyrazolo[1,5-a]pyrazin-5(4H)-yl)ethan-1-one × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;277 K;0.2 M Sodium Chloride, 0.1M HEPES pH 7.5, 25% (w/v) PEG 3350 Resolution 2.50 Å R-free 0.294

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.

278 other PDB entries and 429 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name UBB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–75; UniProt 1–75 Author chain C; PDBConstruct 1–75; UniProt 1–75

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 8w31

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8w31
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8w31
Deposition date deposition_date2024-02-21
Structure title titleCrystal structure of parkin (R0RB):2pUb with activator compound
Keywords keywordsE3-ubiquitin ligase, LIGASE, activator; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.44
Radius of gyration Rg (electron density) rg_electron24.62
Forward intensity I(0) i034912700.00
Molecular weight molecular_weight43523.0 kDa
Excluded volume excluded_volume53657 ų
Envelope volume envelope_volume66525 ų
Hydration-shell volume shell_volume23922 ų
Envelope diameter envelope_diameter94.5
Shell Rg shell_rg30.12
Envelope Rg envelope_rg24.96
Shape Rg shape_rg24.57
Total Rg total_rg25.39
Total atoms total_atoms3019
Residues n_residues378
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 dmax91.5
Rg (real space) rg_real25.57
Rg uncertainty (real space) rg_real_error0.88
I(0) (real space) i0_real3.4910e+07
I(0) uncertainty (real space) i0_real_error5.5460e+05
Rg (reciprocal space) rg_reciprocal25.53
I(0) (reciprocal space) i0_reciprocal34910000.0000
Solution quality estimate total_estimate0.6445
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.6
Skewness Skewness skewness0.533
Kurtosis Kurtosis kurtosis0.024
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5173000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.704; Stabil: 1.000; Sysdev: 0.164; Positv: 1.000; Valcen: 0.874; Smooth: 0.897

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)