4jjy

Alix V domain

Method: X-RAY DIFFRACTION Dmax: 160.4 Å Quality: REASONABLE

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

Programmed cell death 6-interacting protein

Homo sapiens

UniProt Q8WUM4

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 355–708 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;277 K;0.1 M sodium citrate pH 5, 6-8% PEG 8000, 5-10% ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 6.50 Å R-free 0.283
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 355–708 Non-standard monomer:Yes (specific site not provided by mmCIF) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 5;277 K;0.1 M sodium citrate pH 5, 6-8% PEG 8000, 5-10% ethylene glycol, VAPOR DIFFUSION, HANGING DROP, temperature 277K Resolution 6.50 Å R-free 0.283

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.

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

View Construct and Data Evidence
UniProt name PDC6I_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 6–360; UniProt 355–708 Author chain B; PDBConstruct 6–360; UniProt 355–708

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 4jjy

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4jjy
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4jjy
Deposition date deposition_date2013-03-08
Structure title titleAlix V domain
Keywords keywordsUbiquitin, Endosome, Membrane Trafficking, virus budding, ESCRTI, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier45.23
Radius of gyration Rg (electron density) rg_electron45.48
Forward intensity I(0) i096988500.00
Molecular weight molecular_weight77210.0 kDa
Excluded volume excluded_volume95933 ų
Envelope volume envelope_volume177170 ų
Hydration-shell volume shell_volume36333 ų
Envelope diameter envelope_diameter158.0
Shell Rg shell_rg44.03
Envelope Rg envelope_rg44.04
Shape Rg shape_rg45.42
Total Rg total_rg45.58
Total atoms total_atoms5396
Residues n_residues676
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 dmax160.4
Rg (real space) rg_real45.56
Rg uncertainty (real space) rg_real_error2.45
I(0) (real space) i0_real9.6990e+07
I(0) uncertainty (real space) i0_real_error1.9200e+06
Rg (reciprocal space) rg_reciprocal45.24
I(0) (reciprocal space) i0_reciprocal96950000.0000
Solution quality estimate total_estimate0.5953
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary50.4
Skewness Skewness skewness0.428
Kurtosis Kurtosis kurtosis-0.281
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3813000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.654; Stabil: 1.000; Sysdev: 0.010; Positv: 1.000; Valcen: 0.901; Smooth: 0.842

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)