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Crystal structure analysis of human E-cadherin (1-213)

Analyse Crystal structure analysis of human E-cadherin (1-213) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2O72
Type: protein
Length: 213 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Epithelial-cadherin
UniProt: P12830
Ligands: CA
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 1 distinct chain · 2% helix, 44% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Epithelial-cadherin	protein	213	2% helix, 44% strand	P12830

Ligands and binding sites

CA · Calcium ion · metal · 5 copies · chains A

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

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	54	0.34	0.78	15	empty

Compared structures

2O72 · Crystal Structure Analysis of human E-cadherin (1-213) · the same entry in another collection · chain A against A, TM-score 1.00
P12830 · AlphaFold monomer V2.0 prediction for cadherin-1 (P12830) · a predicted model of the same protein · chain A against A, TM-score 0.97

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 P12830
Elsewhere: RCSB PDB 2O72 · PDBe 2O72 · UniProt P12830

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