6n8r

Crystal structure of the human cell polarity protein Lethal Giant Larvae 2 (Lgl2). aPKC phosphorylated, crystal form 2.

Method: X-RAY DIFFRACTION Dmax: 109.1 Å Quality: GOOD

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

Lethal(2) giant larvae protein homolog 2

Homo sapiens

UniProt Q6P1M3

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 13–978 Not recorded CL CHLORIDE ION × 1 GOL GLYCEROL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8;295.15 K;25% PEG 1500, 100 mM SPG pH 8.0 Resolution 1.91 Å R-free 0.219

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.

9 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name L2GL2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–967; UniProt 13–978

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 6n8r

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6n8r
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6n8r
Deposition date deposition_date2018-11-30
Structure title titleCrystal structure of the human cell polarity protein Lethal Giant Larvae 2 (Lgl2). aPKC phosphorylated, crystal form 2.
Keywords keywordsLgl, Polarity, beta propeller, LIPID BINDING PROTEIN; LIPID BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier32.55
Radius of gyration Rg (electron density) rg_electron31.99
Forward intensity I(0) i0129467000.00
Molecular weight molecular_weight91752.0 kDa
Excluded volume excluded_volume115290 ų
Envelope volume envelope_volume144730 ų
Hydration-shell volume shell_volume38491 ų
Envelope diameter envelope_diameter113.3
Shell Rg shell_rg38.14
Envelope Rg envelope_rg31.87
Shape Rg shape_rg31.99
Total Rg total_rg32.52
Total atoms total_atoms6479
Residues n_residues831
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 dmax109.1
Rg (real space) rg_real32.70
Rg uncertainty (real space) rg_real_error0.83
I(0) (real space) i0_real1.2950e+08
I(0) uncertainty (real space) i0_real_error2.0460e+06
Rg (reciprocal space) rg_reciprocal32.64
I(0) (reciprocal space) i0_reciprocal129500000.0000
Solution quality estimate total_estimate0.8592
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.4
Skewness Skewness skewness0.454
Kurtosis Kurtosis kurtosis-0.390
Angular range angular_range— – 0.2450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha32360000.0000
Real-space data points n_real_points50
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.779; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.962; Smooth: 0.866

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id6n8rA01
Class class2 — Mainly Beta
Architecture architecture130 — 7 Propeller
Topology topology10 — Methylamine Dehydrogenase; Chain H
Homologous superfamily homologous superfamily10 — YVTN repeat-like/Quinoprotein amine dehydrogenase

8. Citations (1)

9. Files and Curves (10)