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Bombyx mori GH13 sucrose hydrolase mutant E322Q covalent intermediate

Analyse Bombyx mori GH13 sucrose hydrolase mutant E322Q covalent intermediate in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6LGH
Type
protein
Length
1,133 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Sucrose hydrolase
UniProt
A0A077JI83
Ligands
BGC, MG, CA
Pockets
11 · best druggability 0.71

Structure

x-ray diffraction · 2 distinct chains · 30% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ASucrose hydrolaseprotein56530% helix, 20% strandA0A077JI83
BSucrose hydrolaseprotein56829% helix, 20% strandA0A077JI83

Ligands and binding sites

  • BGC · beta-D-glucopyranose · sugar · 2 copies · chains A, B
  • MG · Magnesium ion · metal · 2 copies · chains A, B
  • CA · Calcium ion · metal · 2 copies · chains A, B

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

Pockets

11 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15710.710.8043empty
22960.620.8044BGC
33170.620.7942BGC
42970.540.7644empty
52540.540.7629empty

Interfaces

1 interface between chains.

  • A–B · 1257 Ų buried · 22 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 2 glycan (glycosylation).

Compared structures

  • 6LGH · Bombyx mori GH13 sucrose hydrolase mutant E322Q covalent intermediate · the same entry in another collection · chain A against A, TM-score 1.00

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