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Structural basis of cell-cell adhesion by cadherins

Analyse Structural basis of cell-cell adhesion by cadherins in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1NCI
Type: protein
Length: 198 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: N-cadherin
UniProt: P15116
Ligands: IUM
Pockets: 1 · best druggability 0.38

Structure

x-ray diffraction · 2 distinct chains · 2% helix, 43% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	N-cadherin	protein	102	4% helix, 41% strand	P15116
B	N-cadherin	protein	96	0% helix, 46% strand	P15116

Ligands and binding sites

IUM · Uranyl (VI) ion · ligand · 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	99	0.38	0.75	20	empty

Interfaces

1 interface between chains.

A–B · 970 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

1NCI · Structural basis of cell-cell adhesion by cadherins · the same entry in another collection · chain A against A, TM-score 1.00
P15116 · AlphaFold monomer V2.0 prediction for cadherin-2 (P15116) · a predicted model of the same protein · chain B 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 P15116
Elsewhere: RCSB PDB 1NCI · PDBe 1NCI · UniProt P15116

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