1ff5

STRUCTURE OF E-CADHERIN DOUBLE DOMAIN

Method: X-RAY DIFFRACTION Dmax: 102.1 Å Quality: GOOD

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

EPITHELIAL CADHERIN

Mus musculus

UniProt P09803

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 157–374 Chain B; UniProt 157–374 Fragment:DOUBLE DOMAIN CA CALCIUM ION × 6 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8.5;298 K;50 mM ammonium sulfate, 50 mM NaOAc, 30% PEG 8000, pH 8.5, Tris-HCl, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K Resolution 2.93 Å

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 25 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CADH1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–219; UniProt 157–374 Author chain B; PDBConstruct 2–219; UniProt 157–374

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 1ff5

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ff5
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ff5
Deposition date deposition_date2000-07-25
Structure title titleSTRUCTURE OF E-CADHERIN DOUBLE DOMAIN
Keywords keywordsE-cadherin, Ca-binding, 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_guinier30.39
Radius of gyration Rg (electron density) rg_electron30.10
Forward intensity I(0) i038779300.00
Molecular weight molecular_weight48008.0 kDa
Excluded volume excluded_volume59833 ų
Envelope volume envelope_volume78345 ų
Hydration-shell volume shell_volume23924 ų
Envelope diameter envelope_diameter100.8
Shell Rg shell_rg33.47
Envelope Rg envelope_rg30.71
Shape Rg shape_rg30.13
Total Rg total_rg30.34
Total atoms total_atoms3368
Residues n_residues438
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 dmax102.1
Rg (real space) rg_real30.59
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real3.8780e+07
I(0) uncertainty (real space) i0_real_error5.6090e+05
Rg (reciprocal space) rg_reciprocal30.51
I(0) (reciprocal space) i0_reciprocal38780000.0000
Solution quality estimate total_estimate0.8619
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary35.4
Skewness Skewness skewness0.412
Kurtosis Kurtosis kurtosis-0.478
Angular range angular_range— – 0.2600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2598000.0000
Real-space data points n_real_points53
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.874; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.762; Smooth: 0.815

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_idd1ff5a1
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_idd1ff5a2
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_idd1ff5b1
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_idd1ff5b2
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_id1ff5A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id1ff5A02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id1ff5B01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins
Domain ID domain_id1ff5B02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily60 — Cadherins

8. Citations (1)

9. Files and Curves (10)