GL1X · GenesisL1 explorer

Research workbench

Structure of human gliomedin

Analyse Structure of human gliomedin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5YBY
Type
protein
Length
245 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Gliomedin
UniProt
Q6ZMI3
Ligands
NAG, NA, CA, PO4

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 55% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGliomedinprotein2455% helix, 55% strandQ6ZMI3

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 3 copies · chains A
  • NA · Sodium ion · metal · 4 copies · chains A
  • CA · Calcium ion · metal · 2 copies · chains A
  • PO4 · Phosphate ion · ion · chains A
  • EDO · 1,2-ethanediol · additive · 2 copies · chains A

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

Modifications

Observed in the structure: 3 glycan (N-glycosylation).

Compared structures

  • 5YBY · Structure of human Gliomedin · the same entry in another collection · chain A against A, TM-score 1.00
  • Q6ZMI3 · AlphaFold monomer V2.0 prediction for gliomedin (Q6ZMI3) · a predicted model of the same protein · chain A against A, TM-score 1.00

Analyse

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