7u3k

GID4 in complex with compound 89

Method: X-RAY DIFFRACTION Dmax: 57.3 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 124–289 Not recorded L73 N-butylglycyl-4-tert-butyl-D-phenylalanyl-3-methoxy-N-methyl-L-phenylalaninamide × 1 GOL GLYCEROL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;20% PEG6000, 0.1 M HEPES, 0.2 M calcium chloride Resolution 2.20 Å R-free 0.313

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 2–167; UniProt 124–289

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 7u3k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7u3k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7u3k
Deposition date deposition_date2022-02-27
Structure title titleGID4 in complex with compound 89
Keywords keywordsComplex, Inhibitor, Protein degradation, PEPTIDE BINDING PROTEIN, PEPTIDE BINDING PROTEIN-INHIBITOR complex; PEPTIDE BINDING PROTEIN/INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier16.66
Radius of gyration Rg (electron density) rg_electron15.31
Forward intensity I(0) i05832620.00
Molecular weight molecular_weight17892.0 kDa
Excluded volume excluded_volume22455 ų
Envelope volume envelope_volume26089 ų
Hydration-shell volume shell_volume14314 ų
Envelope diameter envelope_diameter55.6
Shell Rg shell_rg21.32
Envelope Rg envelope_rg15.84
Shape Rg shape_rg15.30
Total Rg total_rg16.52
Total atoms total_atoms1277
Residues n_residues162
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 dmax57.3
Rg (real space) rg_real16.57
Rg uncertainty (real space) rg_real_error0.37
I(0) (real space) i0_real5.8330e+06
I(0) uncertainty (real space) i0_real_error6.9140e+04
Rg (reciprocal space) rg_reciprocal16.58
I(0) (reciprocal space) i0_reciprocal5833000.0000
Solution quality estimate total_estimate0.8534
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary20.9
Skewness Skewness skewness0.257
Kurtosis Kurtosis kurtosis-0.138
Angular range angular_range— – 0.4800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1541000.0000
Real-space data points n_real_points78
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.697; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 1.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)