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Crystal structure of mouse N-cadherin EC1-2 with aa insertion between residues 2 and 3

Analyse Crystal structure of mouse N-cadherin EC1-2 with aa insertion between residues… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4NUP
Type
protein
Length
651 residues
Chains
3
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
N-cadherin EC1-2
UniProt
Q3UIC2
Ligands
CA
Pockets
6 · best druggability 0.62

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 44% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, CN-cadherin EC1-2protein2175% helix, 44% strandQ3UIC2

Ligands and binding sites

  • CA · Calcium ion · metal · 10 copies · chains A, B, C

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
12380.620.8135empty
22790.590.7840empty
31790.460.7530empty
41470.420.7532empty
5620.400.8016empty

Interfaces

2 interfaces between chains.

  • A–B · 1722 Ų buried · 22 hydrogen bonds · protein-protein
  • A–C · 466 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 4NUP · Crystal structure of mouse N-cadherin EC1-2 with AA insertion between residues 2 and 3 · the same entry in another collection · chain A against A, TM-score 1.00

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