8t31

Crystal structure of GABARAP in complex with the LIR of TP53INP2/DOR

Method: X-RAY DIFFRACTION Dmax: 99.4 Å Quality: GOOD

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

Gamma-aminobutyric acid receptor-associated protein

Homo sapiens

UniProt O95166

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 1–117 Not recorded Tumor protein p53-inducible nuclear protein 2 × 1 (Q8IXH6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;25% PEG3350, 0.1M Na-citrate, 5% isopropanol Resolution 2.10 Å R-free 0.264
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–117 Not recorded Tumor protein p53-inducible nuclear protein 2 × 1 (Q8IXH6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;25% PEG3350, 0.1M Na-citrate, 5% isopropanol Resolution 2.10 Å R-free 0.264
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–117 Not recorded Tumor protein p53-inducible nuclear protein 2 × 1 (Q8IXH6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;25% PEG3350, 0.1M Na-citrate, 5% isopropanol Resolution 2.10 Å R-free 0.264
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1–117 Not recorded Tumor protein p53-inducible nuclear protein 2 × 1 (Q8IXH6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;25% PEG3350, 0.1M Na-citrate, 5% isopropanol Resolution 2.10 Å R-free 0.264
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 1–117 Not recorded Tumor protein p53-inducible nuclear protein 2 × 1 (Q8IXH6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;25% PEG3350, 0.1M Na-citrate, 5% isopropanol Resolution 2.10 Å R-free 0.264

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.

41 other PDB entries and 80 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBRAP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–119; UniProt 1–117 Author chain C; PDBConstruct 3–119; UniProt 1–117 Author chain E; PDBConstruct 3–119; UniProt 1–117 Author chain G; PDBConstruct 3–119; UniProt 1–117 Author chain I; PDBConstruct 3–119; UniProt 1–117

Tumor protein p53-inducible nuclear protein 2

Homo sapiens

UniProt Q8IXH6

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 B; UniProt 31–43 Not recorded Gamma-aminobutyric acid receptor-associated protein × 1 (O95166) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;25% PEG3350, 0.1M Na-citrate, 5% isopropanol Resolution 2.10 Å R-free 0.264
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 31–43 Not recorded Gamma-aminobutyric acid receptor-associated protein × 1 (O95166) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;25% PEG3350, 0.1M Na-citrate, 5% isopropanol Resolution 2.10 Å R-free 0.264
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 31–43 Not recorded Gamma-aminobutyric acid receptor-associated protein × 1 (O95166) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;25% PEG3350, 0.1M Na-citrate, 5% isopropanol Resolution 2.10 Å R-free 0.264
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 31–43 Not recorded Gamma-aminobutyric acid receptor-associated protein × 1 (O95166) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;25% PEG3350, 0.1M Na-citrate, 5% isopropanol Resolution 2.10 Å R-free 0.264
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain J; UniProt 31–43 Not recorded Gamma-aminobutyric acid receptor-associated protein × 1 (O95166) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;25% PEG3350, 0.1M Na-citrate, 5% isopropanol Resolution 2.10 Å R-free 0.264

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.

5 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name T53I2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–15; UniProt 31–43 Author chain D; PDBConstruct 3–15; UniProt 31–43 Author chain F; PDBConstruct 3–15; UniProt 31–43 Author chain H; PDBConstruct 3–15; UniProt 31–43 Author chain J; PDBConstruct 3–15; UniProt 31–43

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 8t31

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8t31
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8t31
Deposition date deposition_date2023-06-07
Structure title titleCrystal structure of GABARAP in complex with the LIR of TP53INP2/DOR
Keywords keywordsAutophagy, GABARAP selectivity, DOR LIR, TP53INP2 LIR, 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_guinier28.60
Radius of gyration Rg (electron density) rg_electron27.71
Forward intensity I(0) i079504500.00
Molecular weight molecular_weight73901.0 kDa
Excluded volume excluded_volume94197 ų
Envelope volume envelope_volume115900 ų
Hydration-shell volume shell_volume35013 ų
Envelope diameter envelope_diameter105.1
Shell Rg shell_rg34.85
Envelope Rg envelope_rg27.58
Shape Rg shape_rg27.68
Total Rg total_rg28.59
Total atoms total_atoms5242
Residues n_residues624
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 dmax99.4
Rg (real space) rg_real28.55
Rg uncertainty (real space) rg_real_error0.67
I(0) (real space) i0_real7.9500e+07
I(0) uncertainty (real space) i0_real_error9.7900e+05
Rg (reciprocal space) rg_reciprocal28.57
I(0) (reciprocal space) i0_reciprocal79510000.0000
Solution quality estimate total_estimate0.8687
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.1
Skewness Skewness skewness0.305
Kurtosis Kurtosis kurtosis-0.251
Angular range angular_range— – 0.2750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29860000.0000
Real-space data points n_real_points56
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.773; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.999

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)