9kzc

Cryo-EM structure of the LGI1 LRR-LGI1 EPTP-ADAM22 ECD complex

Method: ELECTRON MICROSCOPY Dmax: 109.6 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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 233–718 Fragment:UNP RESIDUES 233-729 Leucine-rich glioma-inactivated protein 1 × 2 (O95970) CA CALCIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.78 Å

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 22 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

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 37–557 Chain D; UniProt 37–557 Fragment:UNP RESIDUES 37-557 Mutation:R470A Disintegrin and metalloproteinase domain-containing protein 22 × 1 (Q9P0K1) CA CALCIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.78 Å

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 20 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 B; PDBConstruct 17–537; UniProt 37–557 Author chain D; PDBConstruct 17–537; UniProt 37–557

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 9kzc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9kzc
Deposition date deposition_date2024-12-10
Structure title titleCryo-EM structure of the LGI1 LRR-LGI1 EPTP-ADAM22 ECD complex
Keywords keywordsepilepsy, synapse, adam, eptp, ed40, cell adhesion; CELL ADHESION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier33.96
Radius of gyration Rg (electron density) rg_electron33.15
Forward intensity I(0) i0200452000.00
Molecular weight molecular_weight112020.0 kDa
Excluded volume excluded_volume139480 ų
Envelope volume envelope_volume181500 ų
Hydration-shell volume shell_volume45663 ų
Envelope diameter envelope_diameter113.2
Shell Rg shell_rg39.88
Envelope Rg envelope_rg33.21
Shape Rg shape_rg33.12
Total Rg total_rg33.77
Total atoms total_atoms7846
Residues n_residues993
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 dmax109.6
Rg (real space) rg_real33.91
Rg uncertainty (real space) rg_real_error0.64
I(0) (real space) i0_real2.0050e+08
I(0) uncertainty (real space) i0_real_error3.0160e+06
Rg (reciprocal space) rg_reciprocal33.94
I(0) (reciprocal space) i0_reciprocal200500000.0000
Solution quality estimate total_estimate0.8979
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary39.6
Skewness Skewness skewness0.281
Kurtosis Kurtosis kurtosis-0.478
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha22440000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.916; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.925

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)