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Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase from amycolatopsis mediterranei (AMGH128_I)

Analyse Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6UAQ
Type
protein
Length
241 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
GLYCO_HYDRO_CC domain-containing protein
UniProt
G0FQ07
Ligands
NA
Pockets
1 · best druggability 0.33

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGLYCO_HYDRO_CC domain-containing proteinprotein24136% helix, 20% strandG0FQ07

Ligands and binding sites

  • NA · Sodium ion · metal · chains A
  • GOL · Glycerol · additive · 3 copies · 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
1770.330.7420GOL

Compared structures

  • 6UAQ · Crystal structure of a GH128 (subgroup I) endo-beta-1,3-glucanase from Amycolatopsis… · the same entry in another collection · chain A against A, TM-score 1.00

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