1iyf

Solution structure of ubiquitin-like domain of human parkin

Method: SOLUTION NMR Dmax: 45.5 Å Quality: GOOD

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–76 Fragment:ubiquitin-like domain No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6;303 K;Ionic strength (raw mmCIF value) 0.3;Pressure 1 NMR measurement conditions:pH 6;310 K;Ionic strength (raw mmCIF value) 0.3;Pressure 1 NMR sample composition:0.1mM parkin ubiquitin-like domain U-15N, 13C; 50mM potassium phosphate buffer | 90% H2O/10% D2O NMR sample composition:0.1mM parkin ubiquitin-like domain U-15N, 13C; 50mM potassium phosphate buffer | 90% H2O, 10% D2O, 5%-DMPC/DHPC; 90% H2O, 10% D2O, 5%-DMPC/DHPC/CTAB Resolution not provided

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 6–81; 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 1iyf

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1iyf
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1iyf
Deposition date deposition_date2002-08-13
Structure title titleSolution structure of ubiquitin-like domain of human parkin
Keywords keywordsUbiquitin fold, RIKEN Structural Genomics/Proteomics Initiative, RSGI, Structural Genomics, LIGASE; LIGASE
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier11.94
Radius of gyration Rg (electron density) rg_electron11.66
Forward intensity I(0) i0110947000.00
Molecular weight molecular_weight88081.0 kDa
Excluded volume excluded_volume110430 ų
Envelope volume envelope_volume18568 ų
Hydration-shell volume shell_volume11547 ų
Envelope diameter envelope_diameter49.5
Shell Rg shell_rg19.58
Envelope Rg envelope_rg14.54
Shape Rg shape_rg11.65
Total Rg total_rg12.01
Total atoms total_atoms12450
Residues n_residues760
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 dmax45.5
Rg (real space) rg_real11.94
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real1.1090e+08
I(0) uncertainty (real space) i0_real_error1.2740e+06
Rg (reciprocal space) rg_reciprocal11.94
I(0) (reciprocal space) i0_reciprocal110900000.0000
Solution quality estimate total_estimate0.8001
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary14.4
Skewness Skewness skewness0.410
Kurtosis Kurtosis kurtosis0.207
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha209100.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.512; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.879; Smooth: 0.981

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1iyfa_
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_id1iyfA00
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)