5y31

Crystal structure of human LGI1-ADAM22 complex

Method: X-RAY DIFFRACTION Dmax: 190.4 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 233–729 Fragment:UNP RESIDUES 233-729 Leucine-rich glioma-inactivated protein 1 × 1 (O95970) CA CALCIUM ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;10 % PEG 8000, 0.1 M zinc acetate, 0.1 M MES-Na (pH 6.0) Resolution 7.12 Å R-free 0.316
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 233–729 Fragment:UNP RESIDUES 233-729 Leucine-rich glioma-inactivated protein 1 × 1 (O95970) CA CALCIUM ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;10 % PEG 8000, 0.1 M zinc acetate, 0.1 M MES-Na (pH 6.0) Resolution 7.12 Å R-free 0.316

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 1–497; UniProt 233–729 Author chain C; 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 37–557 Fragment:UNP RESIDUES 37-557 Mutation:R470A Disintegrin and metalloproteinase domain-containing protein 22 × 1 (Q9P0K1) CA CALCIUM ION × 4 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;10 % PEG 8000, 0.1 M zinc acetate, 0.1 M MES-Na (pH 6.0) Resolution 7.12 Å R-free 0.316
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count 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 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 5 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;10 % PEG 8000, 0.1 M zinc acetate, 0.1 M MES-Na (pH 6.0) Resolution 7.12 Å R-free 0.316

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 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 5y31

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5y31
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5y31
Deposition date deposition_date2017-07-27
Structure title titleCrystal structure of human LGI1-ADAM22 complex
Keywords keywordsepilepsy, synapse, ADAM, EPTP, WD40, CELL ADHESION; CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier55.61
Radius of gyration Rg (electron density) rg_electron55.51
Forward intensity I(0) i0756314000.00
Molecular weight molecular_weight226070.0 kDa
Excluded volume excluded_volume281460 ų
Envelope volume envelope_volume414790 ų
Hydration-shell volume shell_volume66027 ų
Envelope diameter envelope_diameter206.3
Shell Rg shell_rg52.43
Envelope Rg envelope_rg55.56
Shape Rg shape_rg55.39
Total Rg total_rg55.83
Total atoms total_atoms15832
Residues n_residues1986
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 dmax190.4
Rg (real space) rg_real56.23
Rg uncertainty (real space) rg_real_error2.83
I(0) (real space) i0_real7.5630e+08
I(0) uncertainty (real space) i0_real_error1.5490e+07
Rg (reciprocal space) rg_reciprocal55.07
I(0) (reciprocal space) i0_reciprocal755000000.0000
Solution quality estimate total_estimate0.7772
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary47.6
Skewness Skewness skewness0.559
Kurtosis Kurtosis kurtosis-0.392
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha64190000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.680; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.727; Smooth: 0.332

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)