5y30

Crystal structure of LGI1 LRR domain

Method: X-RAY DIFFRACTION Dmax: 62.6 Å Quality: GOOD

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

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 37–223 Fragment:LGI1 LRR domain (UNP RESIDUES 37-223) No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.5;293 K;20% PEG 4000, 0.2 M ammonium acetate, 0.1 M tri-sodium citrate (pH 5.5) Resolution 1.78 Å R-free 0.191

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 1
Chains and sequence ranges Author chain A; PDBConstruct 17–203; UniProt 37–223

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 5y30

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5y30
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5y30
Deposition date deposition_date2017-07-27
Structure title titleCrystal structure of LGI1 LRR domain
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_guinier18.25
Radius of gyration Rg (electron density) rg_electron17.08
Forward intensity I(0) i07623300.00
Molecular weight molecular_weight20419.0 kDa
Excluded volume excluded_volume25660 ų
Envelope volume envelope_volume29611 ų
Hydration-shell volume shell_volume15113 ų
Envelope diameter envelope_diameter64.8
Shell Rg shell_rg22.57
Envelope Rg envelope_rg17.45
Shape Rg shape_rg17.01
Total Rg total_rg18.23
Total atoms total_atoms1436
Residues n_residues182
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 dmax62.6
Rg (real space) rg_real18.25
Rg uncertainty (real space) rg_real_error0.49
I(0) (real space) i0_real7.6230e+06
I(0) uncertainty (real space) i0_real_error1.0430e+05
Rg (reciprocal space) rg_reciprocal18.25
I(0) (reciprocal space) i0_reciprocal7623000.0000
Solution quality estimate total_estimate0.7831
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.0
Skewness Skewness skewness0.386
Kurtosis Kurtosis kurtosis-0.104
Angular range angular_range— – 0.4350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha877000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.728; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd5y30a_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.10 — Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
Superfamily Superfamily superfamilyc.10.2 — L domain-like
Family Family familyc.10.2.0 — automated matches

8. Citations (1)

9. Files and Curves (10)