8y6b

Structure of human LGI1-ADAM22 complex in space group P212121

Method: X-RAY DIFFRACTION Dmax: 226.0 Å Quality: GOOD

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

Disintegrin and metalloproteinase domain-containing protein 22

Homo sapiens

UniProt Q9P0K1

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 233–718 Not recorded Leucine-rich glioma-inactivated protein 1 × 1 (O95970) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;0.8M sodium/potassium tartrate, 0.1M Tris pH=7.0, 0.2M lithium sulfate. Resolution 3.49 Å R-free 0.277
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 233–718 Not recorded Leucine-rich glioma-inactivated protein 1 × 1 (O95970) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;0.8M sodium/potassium tartrate, 0.1M Tris pH=7.0, 0.2M lithium sulfate. Resolution 3.49 Å R-free 0.277
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 233–718 Not recorded Leucine-rich glioma-inactivated protein 1 × 1 (O95970) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;0.8M sodium/potassium tartrate, 0.1M Tris pH=7.0, 0.2M lithium sulfate. Resolution 3.49 Å R-free 0.277

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 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ADA22_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–486; UniProt 233–718 Author chain B; PDBConstruct 1–486; UniProt 233–718 Author chain C; PDBConstruct 1–486; UniProt 233–718

Leucine-rich glioma-inactivated protein 1

Homo sapiens

UniProt O95970

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 39–557 Not recorded Disintegrin and metalloproteinase domain-containing protein 22 × 1 (Q9P0K1) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;0.8M sodium/potassium tartrate, 0.1M Tris pH=7.0, 0.2M lithium sulfate. Resolution 3.49 Å R-free 0.277
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 39–557 Not recorded Disintegrin and metalloproteinase domain-containing protein 22 × 1 (Q9P0K1) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;0.8M sodium/potassium tartrate, 0.1M Tris pH=7.0, 0.2M lithium sulfate. Resolution 3.49 Å R-free 0.277
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 39–557 Not recorded Disintegrin and metalloproteinase domain-containing protein 22 × 1 (Q9P0K1) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 CA CALCIUM ION × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;293 K;0.8M sodium/potassium tartrate, 0.1M Tris pH=7.0, 0.2M lithium sulfate. Resolution 3.49 Å R-free 0.277

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.

8 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name LGI1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 8–526; UniProt 39–557 Author chain E; PDBConstruct 8–526; UniProt 39–557 Author chain F; PDBConstruct 8–526; UniProt 39–557

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 8y6b

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8y6b
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8y6b
Deposition date deposition_date2024-02-02
Structure title titleStructure of human LGI1-ADAM22 complex in space group P212121
Keywords keywordssynaptic modulator, complex, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier80.08
Radius of gyration Rg (electron density) rg_electron82.30
Forward intensity I(0) i01707160000.00
Molecular weight molecular_weight343140.0 kDa
Excluded volume excluded_volume427280 ų
Envelope volume envelope_volume793910 ų
Hydration-shell volume shell_volume90634 ų
Envelope diameter envelope_diameter317.7
Shell Rg shell_rg60.74
Envelope Rg envelope_rg82.22
Shape Rg shape_rg82.47
Total Rg total_rg81.30
Total atoms total_atoms24030
Residues n_residues3009
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 dmax226.0
Rg (real space) rg_real78.17
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real1.6860e+09
I(0) uncertainty (real space) i0_real_error3.2340e+07
Rg (reciprocal space) rg_reciprocal77.64
I(0) (reciprocal space) i0_reciprocal1696000000.0000
Solution quality estimate total_estimate0.8394
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary107.0
Skewness Skewness skewness0.240
Kurtosis Kurtosis kurtosis-0.738
Angular range angular_range— – 0.0950 −1
Current regularization parameter α current_alpha0.0326
Highest regularization parameter α highest_alpha38810000.0000
Real-space data points n_real_points20
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.973; Stabil: 0.992; Sysdev: 1.000; Positv: 1.000; Valcen: 0.947; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)