4zt1

Crystal structure of human E-Cadherin (residues 3-213) in x-dimer conformation

Method: X-RAY DIFFRACTION Dmax: 99.9 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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 157–367 Chain B; UniProt 157–367 Fragment:UNP residues 157-367 CA CALCIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;298 K;TRIS 0.1 M, ammonium sulfate 1.3 M, calcium chloride 50 mM Resolution 1.92 Å R-free 0.219

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 A; PDBConstruct 1–211; UniProt 157–367 Author chain B; PDBConstruct 1–211; UniProt 157–367

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 4zt1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4zt1
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4zt1
Deposition date deposition_date2015-05-14
Structure title titleCrystal structure of human E-Cadherin (residues 3-213) in x-dimer conformation
Keywords keywordsadhesion, cadherin, calcium-binding protein, x-dimer., 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_guinier29.46
Radius of gyration Rg (electron density) rg_electron29.25
Forward intensity I(0) i034870000.00
Molecular weight molecular_weight45451.0 kDa
Excluded volume excluded_volume56692 ų
Envelope volume envelope_volume73616 ų
Hydration-shell volume shell_volume23186 ų
Envelope diameter envelope_diameter101.1
Shell Rg shell_rg32.81
Envelope Rg envelope_rg29.67
Shape Rg shape_rg29.25
Total Rg total_rg29.61
Total atoms total_atoms3186
Residues n_residues418
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 dmax99.9
Rg (real space) rg_real29.62
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real3.4870e+07
I(0) uncertainty (real space) i0_real_error5.4180e+05
Rg (reciprocal space) rg_reciprocal29.55
I(0) (reciprocal space) i0_reciprocal34870000.0000
Solution quality estimate total_estimate0.8694
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary35.1
Skewness Skewness skewness0.406
Kurtosis Kurtosis kurtosis-0.403
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2575000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.861; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.839; Smooth: 0.877

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd4zt1a1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.6 — Cadherin-like
Family Family familyb.1.6.1 — Cadherin
Domain ID domain_idd4zt1a2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.6 — Cadherin-like
Family Family familyb.1.6.1 — Cadherin
Domain ID domain_idd4zt1b1
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.6 — Cadherin-like
Family Family familyb.1.6.1 — Cadherin
Domain ID domain_idd4zt1b2
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.6 — Cadherin-like
Family Family familyb.1.6.1 — Cadherin

CATH v4.4 (4 domains)

Domain ID domain_id4zt1A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id4zt1A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id4zt1B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id4zt1B02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins

8. Citations (1)

9. Files and Curves (10)