GL1X · GenesisL1 explorer

MolNFT v1 · #173257 · protein

Cryo-EM structure of human exostosin-like 3 (EXTL3)

7AU2: “Cryo-EM structure of human exostosin-like 3 (EXTL3)”. Electron microscopy, 3 ligands (NAG, BMA, MAN), 20 pockets (best druggability 0.86). MolNFT v1 #173257 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB
7AU2
Type
protein
Length
1,372 residues
Chains
2
Method
electron microscopy
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Exostosin-like 3
EC
2.4.1.223
UniProt
O43909
Ligands
NAG, BMA, MAN
Pockets
20 · best druggability 0.86

Structure

electron microscopy · 1 distinct chain · 34% helix, 17% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BExostosin-like 3 (EC 2.4.1.223)protein68634% helix, 17% strandO43909

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 8 copies · chains A, B
  • BMA · beta-D-mannopyranose · sugar · 2 copies · chains A, B
  • MAN · alpha-D-mannopyranose · sugar · 2 copies · chains A, B

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

Pockets

20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
18600.860.88115empty
211310.820.8369empty
35980.790.8558empty
41320.740.9424empty
51230.740.9424empty

Interfaces

1 interface between chains.

  • A–B · 4769 Ų buried · 58 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 10 disulfide, 4 glycan (disulfide, N-glycosylation).

Compared structures

  • 7AU2 · Cryo-EM structure of human exostosin-like 3 (EXTL3) · the same entry in another collection · chain A against A, TM-score 1.00
  • O43909 · AlphaFold monomer V2.0 prediction for exostosin-like 3 (O43909) · a predicted model of the same protein · chain A against A, TM-score 0.99

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