5n2w

WT-Parkin and pUB complex

Method: X-RAY DIFFRACTION Dmax: 93.0 Å Quality: GOOD

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

E3 ubiquitin-protein ligase parkin,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 1–83 Chain A; UniProt 144–465 Not recorded Polyubiquitin-B × 1 (P0CG47) ZN ZINC ION × 8 CL CHLORIDE ION × 1 TMO trimethylamine oxide × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;100mM Tris pH 8.5, 200mM TMAO, PEG MME 2000 Resolution 2.68 Å R-free 0.243

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 PRKN2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–83; UniProt 1–83 Author chain A; PDBConstruct 84–405; UniProt 144–465

Polyubiquitin-B

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 × 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,E3 ubiquitin-protein ligase parkin × 1 (O60260) ZN ZINC ION × 8 CL CHLORIDE ION × 1 TMO trimethylamine oxide × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;277 K;100mM Tris pH 8.5, 200mM TMAO, PEG MME 2000 Resolution 2.68 Å R-free 0.243

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 1–76; 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 5n2w

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5n2w
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5n2w
Deposition date deposition_date2017-02-08
Structure title titleWT-Parkin and pUB complex
Keywords keywordsComplex structure of Parkin and pUB, Transferase, ligase; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier26.84
Radius of gyration Rg (electron density) rg_electron25.83
Forward intensity I(0) i051472500.00
Molecular weight molecular_weight52430.0 kDa
Excluded volume excluded_volume64176 ų
Envelope volume envelope_volume81157 ų
Hydration-shell volume shell_volume27284 ų
Envelope diameter envelope_diameter97.9
Shell Rg shell_rg31.91
Envelope Rg envelope_rg26.02
Shape Rg shape_rg25.75
Total Rg total_rg26.68
Total atoms total_atoms3628
Residues n_residues456
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 dmax93.0
Rg (real space) rg_real26.87
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real5.1470e+07
I(0) uncertainty (real space) i0_real_error7.6640e+05
Rg (reciprocal space) rg_reciprocal26.86
I(0) (reciprocal space) i0_reciprocal51470000.0000
Solution quality estimate total_estimate0.8705
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary29.9
Skewness Skewness skewness0.377
Kurtosis Kurtosis kurtosis-0.242
Angular range angular_range— – 0.2950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5411000.0000
Real-space data points n_real_points60
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.915; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5n2wb_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.1 — Ubiquitin-related

CATH v4.4 (1 domains)

Domain ID domain_id5n2wA01
Class class3 — Alpha Beta
Architecture architecture10 — Roll
Topology topology20 — Ubiquitin-like (UB roll)
Homologous superfamily homologous superfamily90 — Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

8. Citations (1)

9. Files and Curves (10)