9ok4

GID4 in complex with CLEO4-88 and ACAA1

Method: X-RAY DIFFRACTION Dmax: 92.9 Å Quality: EXCELLENT

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

3-ketoacyl-CoA thiolase, peroxisomal

Homo sapiens

UniProt P09110

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 30–424 Chain B; UniProt 30–424 Not recorded Glucose-induced degradation protein 4 homolog × 2 (Q8IVV7) L6U (2S)-2-{[(2S)-2-({N-[(2,4-dimethoxyphenyl)methyl]glycyl}amino)-2-(thiophen-2-yl)acetyl]amino}-N-methyl-4-phenylbutanamide × 2 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;20% PEG3350, 0.1 M Tris pH 7.5 and 0.2 M NaF Resolution 2.28 Å R-free 0.230

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name THIK_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 24–418; UniProt 30–424 Author chain B; PDBConstruct 24–418; UniProt 30–424

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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain C; UniProt 124–289 Chain D; UniProt 124–289 Not recorded 3-ketoacyl-CoA thiolase, peroxisomal × 2 (P09110) L6U (2S)-2-{[(2S)-2-({N-[(2,4-dimethoxyphenyl)methyl]glycyl}amino)-2-(thiophen-2-yl)acetyl]amino}-N-methyl-4-phenylbutanamide × 2 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;20% PEG3350, 0.1 M Tris pH 7.5 and 0.2 M NaF Resolution 2.28 Å R-free 0.230

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 2
Chains and sequence ranges Author chain C; PDBConstruct 2–167; UniProt 124–289 Author chain D; 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 9ok4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ok4
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ok4
Deposition date deposition_date2025-05-09
Structure title titleGID4 in complex with CLEO4-88 and ACAA1
Keywords keywordsInhibitor, Protein complex, Molecular glue, Thiolase, CTLH complex, E3 ligase, PEPTIDE BINDING PROTEIN; PEPTIDE BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.20
Radius of gyration Rg (electron density) rg_electron30.33
Forward intensity I(0) i0198638000.00
Molecular weight molecular_weight112510.0 kDa
Excluded volume excluded_volume140710 ų
Envelope volume envelope_volume171320 ų
Hydration-shell volume shell_volume45719 ų
Envelope diameter envelope_diameter101.1
Shell Rg shell_rg38.67
Envelope Rg envelope_rg30.17
Shape Rg shape_rg30.42
Total Rg total_rg30.74
Total atoms total_atoms7927
Residues n_residues1087
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 dmax92.9
Rg (real space) rg_real31.00
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real1.9860e+08
I(0) uncertainty (real space) i0_real_error2.9220e+06
Rg (reciprocal space) rg_reciprocal31.09
I(0) (reciprocal space) i0_reciprocal198700000.0000
Solution quality estimate total_estimate0.9104
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.1
Skewness Skewness skewness0.093
Kurtosis Kurtosis kurtosis-0.622
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha55380000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.971; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.927

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)