6yoo

Structure of SAMM50 LIR bound to GABARAPL1

Method: X-RAY DIFFRACTION Dmax: 51.8 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 Sorting and assembly machinery component 50 homolog × 1 (Q9Y512) EDO 1,2-ETHANEDIOL × 2 ZN ZINC ION × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;24% w/v PEG 6000, 10 mM ZnCl2 and 0.1 M Tris pH 7.5 Resolution 1.06 Å R-free 0.147

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 30 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

Sorting and assembly machinery component 50 homolog

Homo sapiens

UniProt Q9Y512

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 24–35 Not recorded Gamma-aminobutyric acid receptor-associated protein-like 1 × 1 (Q9H0R8) EDO 1,2-ETHANEDIOL × 2 ZN ZINC ION × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;24% w/v PEG 6000, 10 mM ZnCl2 and 0.1 M Tris pH 7.5 Resolution 1.06 Å R-free 0.147

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 SAM50_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–12; UniProt 24–35

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 6yoo

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6yoo
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6yoo
Deposition date deposition_date2020-04-14
Structure title titleStructure of SAMM50 LIR bound to GABARAPL1
Keywords keywordsLIR, SAMM50, ATG8, 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_guinier15.59
Radius of gyration Rg (electron density) rg_electron14.16
Forward intensity I(0) i04449730.00
Molecular weight molecular_weight15387.0 kDa
Excluded volume excluded_volume19373 ų
Envelope volume envelope_volume21402 ų
Hydration-shell volume shell_volume12799 ų
Envelope diameter envelope_diameter49.6
Shell Rg shell_rg20.00
Envelope Rg envelope_rg14.46
Shape Rg shape_rg14.10
Total Rg total_rg15.54
Total atoms total_atoms2134
Residues n_residues128
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 dmax51.8
Rg (real space) rg_real15.48
Rg uncertainty (real space) rg_real_error0.35
I(0) (real space) i0_real4.4500e+06
I(0) uncertainty (real space) i0_real_error4.9300e+04
Rg (reciprocal space) rg_reciprocal15.49
I(0) (reciprocal space) i0_reciprocal4450000.0000
Solution quality estimate total_estimate0.8691
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.6
Skewness Skewness skewness0.118
Kurtosis Kurtosis kurtosis-0.335
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1009000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.766; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.996

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd6yooa1
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.15 — beta-Grasp (ubiquitin-like)
Superfamily Superfamily superfamilyd.15.1 — Ubiquitin-like
Family Family familyd.15.1.0 — automated matches
Domain ID domain_idd6yooa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

8. Citations (1)

9. Files and Curves (10)