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Crystal structure of beta-mannanase from a symbiotic protist of the termite Reticulitermes speratus

Analyse Crystal structure of beta-mannanase from a symbiotic protist of the termite… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3WDQ
Type
protein
Length
330 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.3
Source
Symbiotic protist of Reticulitermes speratus
Molecule
Beta-mannanase
EC
3.2.1.78
UniProt
H7CGE2
Ligands
NAG, NA, MG
Pockets
1 · best druggability 0.31

Structure

x-ray diffraction · resolution 1.3 · 1 distinct chain · 37% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-mannanase (EC 3.2.1.78)protein33037% helix, 15% strandH7CGE2

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · chains A
  • NA · Sodium ion · metal · 2 copies · chains A
  • MG · Magnesium ion · metal · 2 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
1720.310.7420empty

Modifications

Observed in the structure: 1 glycan, 1 modified (N-glycosylation, nonstandard).

Compared structures

  • 3WDQ · Crystal structure of beta-mannanase from a symbiotic protist of the termite… · the same entry in another collection · chain A against A, TM-score 1.00

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