8hq2

Crystal structure of human ADAM22 in complex with human LGI1 mutant

Method: X-RAY DIFFRACTION Dmax: 216.8 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) CA CALCIUM ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;7.5% PEG 4000, 0.2M MAGNESIUM CHLORIDE, 0.1M HEPES PH=7.5 Resolution 2.93 Å R-free 0.291
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) CA CALCIUM ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;7.5% PEG 4000, 0.2M MAGNESIUM CHLORIDE, 0.1M HEPES PH=7.5 Resolution 2.93 Å R-free 0.291

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 21 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

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 Mutation:L88N/F89A/R474Q Disintegrin and metalloproteinase domain-containing protein 22 × 1 (Q9P0K1) CA CALCIUM ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;7.5% PEG 4000, 0.2M MAGNESIUM CHLORIDE, 0.1M HEPES PH=7.5 Resolution 2.93 Å R-free 0.291
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 39–557 Mutation:L88N/F89A/R474Q Disintegrin and metalloproteinase domain-containing protein 22 × 1 (Q9P0K1) CA CALCIUM ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7.5;293 K;7.5% PEG 4000, 0.2M MAGNESIUM CHLORIDE, 0.1M HEPES PH=7.5 Resolution 2.93 Å R-free 0.291

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 19 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

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 8hq2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8hq2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8hq2
Deposition date deposition_date2022-12-13
Structure title titleCrystal structure of human ADAM22 in complex with human LGI1 mutant
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_guinier56.30
Radius of gyration Rg (electron density) rg_electron56.85
Forward intensity I(0) i0769688000.00
Molecular weight molecular_weight227910.0 kDa
Excluded volume excluded_volume283730 ų
Envelope volume envelope_volume449500 ų
Hydration-shell volume shell_volume69447 ų
Envelope diameter envelope_diameter227.0
Shell Rg shell_rg55.06
Envelope Rg envelope_rg56.88
Shape Rg shape_rg56.81
Total Rg total_rg56.90
Total atoms total_atoms15958
Residues n_residues2000
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 dmax216.8
Rg (real space) rg_real56.76
Rg uncertainty (real space) rg_real_error3.12
I(0) (real space) i0_real7.6970e+08
I(0) uncertainty (real space) i0_real_error1.7030e+07
Rg (reciprocal space) rg_reciprocal55.93
I(0) (reciprocal space) i0_reciprocal768700000.0000
Solution quality estimate total_estimate0.8182
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary69.7
Skewness Skewness skewness0.567
Kurtosis Kurtosis kurtosis0.277
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29510000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.656; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.824; Smooth: 0.838

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)