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Crystal structure of mycolicibacterium hassiacum glucosylglycerate hydrolase (mhggh) in complex with glycerol

Analyse Crystal structure of mycolicibacterium hassiacum glucosylglycerate hydrolase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5OHC
Type
protein
Length
890 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Hydrolase
UniProt
K5BDL0
Pockets
4 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 6% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BHydrolaseprotein44551% helix, 6% strandK5BDL0

Ligands and binding sites

  • GOL · Glycerol · additive · 10 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19260.830.8585empty
2640.740.9919GOL
3630.730.9819GOL
4540.500.8612empty

Interfaces

1 interface between chains.

  • A–B · 609 Ų buried · 9 hydrogen bonds · protein-protein

Compared structures

  • 5OHC · Crystal structure of Mycolicibacterium hassiacum glucosylglycerate hydrolase (MhGgH) in… · the same entry in another collection · chain A against A, TM-score 1.00
  • K5BDL0 · AlphaFold monomer V2.0 prediction for glucosylglycerate hydrolase (K5BDL0) · a predicted model of the same protein · chain A against A, TM-score 1.00

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