7q50

human Gid4 bound to a Phe/N-peptide

Method: X-RAY DIFFRACTION Dmax: 55.0 Å Quality: GOOD

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

Glucose-induced degradation protein 4 homolog

Homo sapiens

UniProt Q8IVV7

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 121–290 Not recorded FDVSWFMG peptide × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;1.1 M Sodium malonate, 0.3% Jeffamine ED-2001 pH 7, 0.1 M HEPES pH 7 Resolution 3.16 Å R-free 0.293

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.

30 other PDB entries and 41 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GID4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–170; UniProt 121–290

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 7q50

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7q50
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7q50
Deposition date deposition_date2021-11-02
Structure title titlehuman Gid4 bound to a Phe/N-peptide
Keywords keywordsGID, CTLH, ubiquitin, E3 ligase, LIGASE; LIGASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.92
Radius of gyration Rg (electron density) rg_electron15.66
Forward intensity I(0) i06754360.00
Molecular weight molecular_weight19520.0 kDa
Excluded volume excluded_volume24510 ų
Envelope volume envelope_volume27844 ų
Hydration-shell volume shell_volume14949 ų
Envelope diameter envelope_diameter54.9
Shell Rg shell_rg21.68
Envelope Rg envelope_rg16.00
Shape Rg shape_rg15.64
Total Rg total_rg16.78
Total atoms total_atoms1394
Residues n_residues177
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 dmax55.0
Rg (real space) rg_real16.83
Rg uncertainty (real space) rg_real_error0.30
I(0) (real space) i0_real6.7540e+06
I(0) uncertainty (real space) i0_real_error7.0260e+04
Rg (reciprocal space) rg_reciprocal16.85
I(0) (reciprocal space) i0_reciprocal6754000.0000
Solution quality estimate total_estimate0.8761
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.3
Skewness Skewness skewness0.203
Kurtosis Kurtosis kurtosis-0.274
Angular range angular_range— – 0.4700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1610000.0000
Real-space data points n_real_points77
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.819; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.933

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)