7stz

Crystal Structure of Human E-cadherin EC1-5 bound by mouse monoclonal antibody Fab mAb-1_19A11

Method: X-RAY DIFFRACTION Dmax: 228.1 Å Quality: GOOD

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

Cadherin-1

Homo sapiens

UniProt P12830

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 C; UniProt 155–698 Chain D; UniProt 155–698 Not recorded mAb-1_19A11 Heavy Chain × 2 mAb-1_19A11 Light Chain × 2 EDO 1,2-ETHANEDIOL × 5 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 PG4 TETRAETHYLENE GLYCOL × 5 MAN alpha-D-mannopyranose × 3 BMA beta-D-mannopyranose × 12 CA CALCIUM ION × 24 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 7;290 K;HosaA.19747.a.LS31.PC00180 at 11.5 mg/mL was mixed 2:1 (0.2 uL protein and 0.1 uL precipitant) with 0.1M sodium HEPES pH 7.0 and 15% w/v PEG4000 (ProPlex B11) and stored at 14C. The crystal was cryoprotected with 15% ethylene glycol. Tray: 321285b11, puck: ygq5-2. Resolution 2.95 Å R-free 0.208

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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CADH1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain C; PDBConstruct 17–560; UniProt 155–698 Author chain D; PDBConstruct 17–560; UniProt 155–698

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 7stz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7stz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7stz
Deposition date deposition_date2021-11-15
Structure title titleCrystal Structure of Human E-cadherin EC1-5 bound by mouse monoclonal antibody Fab mAb-1_19A11
Keywords keywords;SSGCID, Cadherin-1, cell adhesion, Structural Genomics, Seattle Structural Genomics Center for Infectious Disease, cell adhesion-immune system complex ;; cell adhesion/immune system
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier73.56
Radius of gyration Rg (electron density) rg_electron75.60
Forward intensity I(0) i0606490000.00
Molecular weight molecular_weight200330.0 kDa
Excluded volume excluded_volume248630 ų
Envelope volume envelope_volume457140 ų
Hydration-shell volume shell_volume62832 ų
Envelope diameter envelope_diameter336.8
Shell Rg shell_rg51.98
Envelope Rg envelope_rg83.25
Shape Rg shape_rg75.62
Total Rg total_rg74.83
Total atoms total_atoms14048
Residues n_residues1837
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 dmax228.1
Rg (real space) rg_real70.72
Rg uncertainty (real space) rg_real_error2.13
I(0) (real space) i0_real5.9790e+08
I(0) uncertainty (real space) i0_real_error1.4310e+07
Rg (reciprocal space) rg_reciprocal68.32
I(0) (reciprocal space) i0_reciprocal598800000.0000
Solution quality estimate total_estimate0.7515
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary54.3
Skewness Skewness skewness0.587
Kurtosis Kurtosis kurtosis-0.538
Angular range angular_range— – 0.1050 −1
Current regularization parameter α current_alpha0.0584
Highest regularization parameter α highest_alpha17800000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.016; Oscil: 0.647; Stabil: 0.996; Sysdev: 1.000; Positv: 1.000; Valcen: 0.773; Smooth: 0.012

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (10)

8. Citations (1)

9. Files and Curves (10)