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Beta-1,4-glycanase cex-CD

Analyse Beta-1,4-glycanase cex-CD in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1EXP
Type
protein
Length
312 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-1,4-D-glycanase cex-CD
EC
3.2.1.91, 3.2.1.8
Ligands
G2F, BGC
Pockets
1 · best druggability 0.38

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-1,4-D-glycanase cex-CD (EC 3.2.1.91, 3.2.1.8)protein31246% helix, 20% strand—

Ligands and binding sites

  • G2F · 2-deoxy-2-fluoro-alpha-D-glucopyranose · ligand · chains A
  • BGC · beta-D-glucopyranose · sugar · 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.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11040.380.7517G2F, BGC

Modifications

Observed in the structure: 2 disulfide, 1 covalent (disulfide, covalent ligand).

Compared structures

  • 1EXP · Beta-1,4-glycanase cex-CD · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

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