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Bacteroides uniformis endo-laminarinase BUGH158 from the BETA(1,3)- glucan utilization locus

Analyse Bacteroides uniformis endo-laminarinase BUGH158 from the BETA(1,3)- glucan… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6PAL
Type
protein
Length
803 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Uncharacterized protein
UniProt
A0A412SRH5
Ligands
SO4
Pockets
5 · best druggability 0.77

Structure

x-ray diffraction · 2 distinct chains · 28% helix, 32% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AUncharacterized proteinprotein40427% helix, 32% strandA0A412SRH5
BUncharacterized proteinprotein39928% helix, 31% strandA0A412SRH5

Ligands and binding sites

  • SO4 · Sulfate ion · ion · chains B
  • ACT · Acetate ion · additive · 4 copies · chains A, B

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

Pockets

5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110810.770.7993ACT
29400.770.7987ACT
3930.650.9119empty
4650.340.7716empty
5610.340.7716empty

Interfaces

1 interface between chains.

  • A–B · 1620 Ų buried · 10 hydrogen bonds · protein-protein

Compared structures

  • 6PAL · Bacteroides uniformis endo-laminarinase BuGH158 from the beta(1,3)-glucan utilization… · the same entry in another collection · chain A against A, TM-score 1.00

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