7aa9

Structure of SCOC pT13/pT15 LIR motif bound to GABARAPL1

Method: X-RAY DIFFRACTION Dmax: 113.7 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 pT13/PT15 SCOC LIR × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20% PEG 1500 0.1M TRIS 8 Resolution 1.72 Å R-free 0.261
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–117 Not recorded pT13/PT15 SCOC LIR × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20% PEG 1500 0.1M TRIS 8 Resolution 1.72 Å R-free 0.261
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–117 Not recorded pT13/PT15 SCOC LIR × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20% PEG 1500 0.1M TRIS 8 Resolution 1.72 Å R-free 0.261
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1–117 Not recorded pT13/PT15 SCOC LIR × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20% PEG 1500 0.1M TRIS 8 Resolution 1.72 Å R-free 0.261
5 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain I; UniProt 1–117 Not recorded pT13/PT15 SCOC LIR × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20% PEG 1500 0.1M TRIS 8 Resolution 1.72 Å R-free 0.261
6 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain K; UniProt 1–117 Not recorded pT13/PT15 SCOC LIR × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;20% PEG 1500 0.1M TRIS 8 Resolution 1.72 Å R-free 0.261

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 25 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 7–123; UniProt 1–117 Author chain C; PDBConstruct 7–123; UniProt 1–117 Author chain E; PDBConstruct 7–123; UniProt 1–117 Author chain G; PDBConstruct 7–123; UniProt 1–117 Author chain I; PDBConstruct 7–123; UniProt 1–117 Author chain K; PDBConstruct 7–123; 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 7aa9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7aa9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7aa9
Deposition date deposition_date2020-09-03
Structure title titleStructure of SCOC pT13/pT15 LIR motif bound to GABARAPL1
Keywords keywordsSCOC, ATG8, LIR, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.43
Radius of gyration Rg (electron density) rg_electron31.78
Forward intensity I(0) i0120369000.00
Molecular weight molecular_weight88515.0 kDa
Excluded volume excluded_volume111280 ų
Envelope volume envelope_volume149410 ų
Hydration-shell volume shell_volume40100 ų
Envelope diameter envelope_diameter120.4
Shell Rg shell_rg37.83
Envelope Rg envelope_rg31.10
Shape Rg shape_rg31.76
Total Rg total_rg32.41
Total atoms total_atoms6263
Residues n_residues746
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 dmax113.7
Rg (real space) rg_real32.32
Rg uncertainty (real space) rg_real_error1.31
I(0) (real space) i0_real1.2040e+08
I(0) uncertainty (real space) i0_real_error1.9930e+06
Rg (reciprocal space) rg_reciprocal32.37
I(0) (reciprocal space) i0_reciprocal120400000.0000
Solution quality estimate total_estimate0.8507
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary44.1
Skewness Skewness skewness0.265
Kurtosis Kurtosis kurtosis-0.122
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29430000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.689; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)