9kzt

Cryo-EM structure of the 3:3 LGI1-ADAM22 complex

Method: ELECTRON MICROSCOPY Dmax: 221.7 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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 233–729 Chain C; UniProt 233–729 Chain E; UniProt 233–729 Fragment:UNP RESIDUES 233-729 Leucine-rich glioma-inactivated protein 1 × 3 (O95970) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.79 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 1–497; UniProt 233–729 Author chain C; PDBConstruct 1–497; UniProt 233–729 Author chain E; PDBConstruct 1–497; UniProt 233–729

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 37–557 Chain D; UniProt 37–557 Chain F; UniProt 37–557 Fragment:UNP RESIDUES 37-557 Mutation:R470A Disintegrin and metalloproteinase domain-containing protein 22 × 3 (Q9P0K1) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.79 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 Author chain F; 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 9kzt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9kzt
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9kzt
Deposition date deposition_date2024-12-11
Structure title titleCryo-EM structure of the 3:3 LGI1-ADAM22 complex
Keywords keywordsepilepsy, syanapse, adam, eptp, wd40, cell adhesion; CELL ADHESION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier62.82
Radius of gyration Rg (electron density) rg_electron62.28
Forward intensity I(0) i01632040000.00
Molecular weight molecular_weight335570.0 kDa
Excluded volume excluded_volume417790 ų
Envelope volume envelope_volume623400 ų
Hydration-shell volume shell_volume84693 ų
Envelope diameter envelope_diameter210.5
Shell Rg shell_rg61.62
Envelope Rg envelope_rg61.07
Shape Rg shape_rg62.19
Total Rg total_rg62.56
Total atoms total_atoms23526
Residues n_residues2979
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 dmax221.7
Rg (real space) rg_real62.91
Rg uncertainty (real space) rg_real_error2.38
I(0) (real space) i0_real1.6320e+09
I(0) uncertainty (real space) i0_real_error3.3810e+07
Rg (reciprocal space) rg_reciprocal62.69
I(0) (reciprocal space) i0_reciprocal1631000000.0000
Solution quality estimate total_estimate0.8680
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary88.7
Skewness Skewness skewness0.205
Kurtosis Kurtosis kurtosis-0.662
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0009
Highest regularization parameter α highest_alpha91980000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.814; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.861

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (2)

9. Files and Curves (10)