9jf2

Crystal structure of GABARAPL1 in complex with ATG16L1

Method: X-RAY DIFFRACTION Dmax: 71.8 Å Quality: GOOD

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 Autophagy-related protein 16-1 × 1 (Q676U5) MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;289 K;0.1 M Sodium cacodylate (pH 6.5), 40% v/v MPD, 5% w/v PEG 8000 Resolution 1.76 Å R-free 0.215
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–117 Not recorded Autophagy-related protein 16-1 × 1 (Q676U5) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;289 K;0.1 M Sodium cacodylate (pH 6.5), 40% v/v MPD, 5% w/v PEG 8000 Resolution 1.76 Å R-free 0.215

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 29 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 5–121; UniProt 1–117 Author chain B; PDBConstruct 5–121; UniProt 1–117

Autophagy-related protein 16-1

OrganismNot specified

UniProt Q676U5

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 D; UniProt 235–247 Not recorded Gamma-aminobutyric acid receptor-associated protein-like 1 × 1 (Q9H0R8) MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;289 K;0.1 M Sodium cacodylate (pH 6.5), 40% v/v MPD, 5% w/v PEG 8000 Resolution 1.76 Å R-free 0.215
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 235–247 Not recorded Gamma-aminobutyric acid receptor-associated protein-like 1 × 1 (Q9H0R8) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;289 K;0.1 M Sodium cacodylate (pH 6.5), 40% v/v MPD, 5% w/v PEG 8000 Resolution 1.76 Å R-free 0.215

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 23 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A16L1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–13; UniProt 235–247 Author chain D; PDBConstruct 1–13; UniProt 235–247

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 9jf2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9jf2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9jf2
Deposition date deposition_date2024-09-03
Structure title titleCrystal structure of GABARAPL1 in complex with ATG16L1
Keywords keywordsGABARAPL1, ATG16L1, 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_guinier21.32
Radius of gyration Rg (electron density) rg_electron20.65
Forward intensity I(0) i015871900.00
Molecular weight molecular_weight31009.0 kDa
Excluded volume excluded_volume39138 ų
Envelope volume envelope_volume45791 ų
Hydration-shell volume shell_volume19236 ų
Envelope diameter envelope_diameter74.3
Shell Rg shell_rg26.37
Envelope Rg envelope_rg20.91
Shape Rg shape_rg20.61
Total Rg total_rg21.59
Total atoms total_atoms4309
Residues n_residues264
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 dmax71.8
Rg (real space) rg_real21.38
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real1.5870e+07
I(0) uncertainty (real space) i0_real_error2.1050e+05
Rg (reciprocal space) rg_reciprocal21.37
I(0) (reciprocal space) i0_reciprocal15870000.0000
Solution quality estimate total_estimate0.7838
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary24.3
Skewness Skewness skewness0.467
Kurtosis Kurtosis kurtosis-0.200
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4217000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.746; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.949; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)