8wzn

ParkinK211N in complex with phospho NEDD8

Method: X-RAY DIFFRACTION Dmax: 93.9 Å Quality: REASONABLE

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

E3 ubiquitin-protein ligase parkin

Homo sapiens

UniProt O60260

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 141–465 Mutation:K211N NEDD8 × 1 (Q15843) ZN ZINC ION × 8 PEG DI(HYDROXYETHYL)ETHER × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;291 K;0.1 M, MMT, 7.0, 25% w/v, PEG 1500 Resolution 1.80 Å R-free 0.212

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.

20 other PDB entries and 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PRKN_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–325; UniProt 141–465

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–76 Non-standard monomer:Yes (specific site not provided by mmCIF) E3 ubiquitin-protein ligase parkin × 1 (O60260) ZN ZINC ION × 8 PEG DI(HYDROXYETHYL)ETHER × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;291 K;0.1 M, MMT, 7.0, 25% w/v, PEG 1500 Resolution 1.80 Å R-free 0.212

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 2
Chains and sequence ranges Author chain B; PDBConstruct 2–77; UniProt 1–76

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 8wzn

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8wzn
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8wzn
Deposition date deposition_date2023-11-02
Structure title titleParkinK211N in complex with phospho NEDD8
Keywords keywordsE3 ligase., LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.52
Radius of gyration Rg (electron density) rg_electron24.63
Forward intensity I(0) i036756500.00
Molecular weight molecular_weight43809.0 kDa
Excluded volume excluded_volume53520 ų
Envelope volume envelope_volume66790 ų
Hydration-shell volume shell_volume23767 ų
Envelope diameter envelope_diameter97.8
Shell Rg shell_rg30.16
Envelope Rg envelope_rg25.01
Shape Rg shape_rg24.55
Total Rg total_rg25.49
Total atoms total_atoms3020
Residues n_residues382
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 dmax93.9
Rg (real space) rg_real25.64
Rg uncertainty (real space) rg_real_error0.97
I(0) (real space) i0_real3.6760e+07
I(0) uncertainty (real space) i0_real_error5.3270e+05
Rg (reciprocal space) rg_reciprocal25.60
I(0) (reciprocal space) i0_reciprocal36760000.0000
Solution quality estimate total_estimate0.6458
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.2
Skewness Skewness skewness0.514
Kurtosis Kurtosis kurtosis0.005
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3339000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.692; Stabil: 1.000; Sysdev: 0.164; Positv: 1.000; Valcen: 0.851; Smooth: 0.972

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)