Research workbench

Crystal structure of E-cadherin EC12 K14E

Analyse Crystal structure of E-cadherin EC12 K14E in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3LNE
Type: protein
Length: 213 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Cadherin-1
UniProt: P09803
Ligands: CA

Structure

x-ray diffraction · 1 distinct chain · 1% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Cadherin-1	protein	213	1% helix, 44% strand	P09803

Ligands and binding sites

CA · Calcium ion · metal · 3 copies · chains A
GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

3LNE · Crystal structure of E-cadherin EC12 K14E · the same entry in another collection · chain A against A, TM-score 1.00
P09803 · AlphaFold monomer V2.0 prediction for cadherin-1 (P09803) · a predicted model of the same protein · chain A against A, TM-score 0.96

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P09803
Elsewhere: RCSB PDB 3LNE · PDBe 3LNE · UniProt P09803

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.