GL1X · GenesisL1 explorer

Research workbench

The crystal structure of the second PDZ domain of human DLG3

Analyse The crystal structure of the second PDZ domain of human DLG3 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2FE5
Type
protein
Length
94 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Presynaptic protein SAP102
UniProt
Q92796
Ligands
SO4

Structure

x-ray diffraction · 1 distinct chain · 15% helix, 38% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
APresynaptic protein SAP102protein9415% helix, 38% strandQ92796

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains A
  • GOL · Glycerol · additive · chains A

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

Compared structures

  • 2FE5 · The Crystal Structure of the Second PDZ Domain of Human DLG3 · the same entry in another collection · chain A against A, TM-score 1.00
  • Q92796 · AlphaFold monomer V2.0 prediction for disks large homolog 3 (Q92796) · a predicted model of the same protein · chain A against A, TM-score 0.94

Analyse

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