9hgc

Crystal structure of human GABARAPL1 in complex with cyclic peptide GAB_D8

Method: X-RAY DIFFRACTION Dmax: 89.6 Å Quality: EXCELLENT

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

Gamma-aminobutyric acid receptor-associated protein-like 1

Homo sapiens

UniProt Q9H0R8

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 GAB_D8 × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;0.17 M ammonium sulfate, 25.5% PEG 4000, 15% glycerol Resolution 2.52 Å R-free 0.259
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–117 Not recorded GAB_D8 × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;0.17 M ammonium sulfate, 25.5% PEG 4000, 15% glycerol Resolution 2.52 Å R-free 0.259
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–117 Not recorded GAB_D8 × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;0.17 M ammonium sulfate, 25.5% PEG 4000, 15% glycerol Resolution 2.52 Å R-free 0.259
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1–117 Not recorded GAB_D8 × 1 SO4 SULFATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;0.17 M ammonium sulfate, 25.5% PEG 4000, 15% glycerol Resolution 2.52 Å R-free 0.259

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.

13 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBRL1_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

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 9hgc

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9hgc
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9hgc
Deposition date deposition_date2024-11-19
Structure title titleCrystal structure of human GABARAPL1 in complex with cyclic peptide GAB_D8
Keywords keywordsautophagy-related protein, cyclic peptide, GABARAPL1, inhibitor, 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_guinier28.20
Radius of gyration Rg (electron density) rg_electron27.31
Forward intensity I(0) i063870500.00
Molecular weight molecular_weight63515.0 kDa
Excluded volume excluded_volume79843 ų
Envelope volume envelope_volume101750 ų
Hydration-shell volume shell_volume31349 ų
Envelope diameter envelope_diameter95.0
Shell Rg shell_rg34.33
Envelope Rg envelope_rg26.77
Shape Rg shape_rg27.30
Total Rg total_rg28.13
Total atoms total_atoms4500
Residues n_residues535
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 dmax89.6
Rg (real space) rg_real28.10
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real6.3870e+07
I(0) uncertainty (real space) i0_real_error9.1540e+05
Rg (reciprocal space) rg_reciprocal28.14
I(0) (reciprocal space) i0_reciprocal63870000.0000
Solution quality estimate total_estimate0.9047
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.8
Skewness Skewness skewness0.196
Kurtosis Kurtosis kurtosis-0.523
Angular range angular_range— – 0.2800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha24120000.0000
Real-space data points n_real_points57
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.929; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.972

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (2)

9. Files and Curves (10)