6qlz

IDOL F3ab subdomain

Method: X-RAY DIFFRACTION Dmax: 86.0 Å Quality: GOOD

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

E3 ubiquitin-protein ligase MYLIP

Homo sapiens

UniProt Q8WY64

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 183–283 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;100mM Hepes pH 7.0 10% (w/v) PEG 6000 Resolution 2.34 Å
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 183–283 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;100mM Hepes pH 7.0 10% (w/v) PEG 6000 Resolution 2.34 Å
3 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain C; UniProt 183–283 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;100mM Hepes pH 7.0 10% (w/v) PEG 6000 Resolution 2.34 Å

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.

34 other PDB entries and 68 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYLIP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–101; UniProt 183–283 Author chain B; PDBConstruct 1–101; UniProt 183–283 Author chain C; PDBConstruct 1–101; UniProt 183–283

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 6qlz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6qlz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6qlz
Deposition date deposition_date2019-02-01
Structure title titleIDOL F3ab subdomain
Keywords keywordsE3 LIGASE CHOLESTEROL METABOLISM LDLR degradation, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier23.77
Radius of gyration Rg (electron density) rg_electron22.93
Forward intensity I(0) i017003300.00
Molecular weight molecular_weight31319.0 kDa
Excluded volume excluded_volume39401 ų
Envelope volume envelope_volume52065 ų
Hydration-shell volume shell_volume19980 ų
Envelope diameter envelope_diameter89.7
Shell Rg shell_rg28.33
Envelope Rg envelope_rg23.11
Shape Rg shape_rg22.91
Total Rg total_rg23.75
Total atoms total_atoms2202
Residues n_residues285
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 dmax86.0
Rg (real space) rg_real23.81
Rg uncertainty (real space) rg_real_error0.91
I(0) (real space) i0_real1.7000e+07
I(0) uncertainty (real space) i0_real_error2.6920e+05
Rg (reciprocal space) rg_reciprocal23.80
I(0) (reciprocal space) i0_reciprocal17000000.0000
Solution quality estimate total_estimate0.7616
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.8
Skewness Skewness skewness0.353
Kurtosis Kurtosis kurtosis-0.338
Angular range angular_range— – 0.3350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3230000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.696; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.813; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)