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Crystal structure of glucosidase from croceicoccus marinus at 1.8 ångström resolution

Analyse Crystal structure of glucosidase from croceicoccus marinus at 1.8 ångström… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5Z3K
Type
protein
Length
957 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Glucosidase
UniProt
A0A1Z1FG87
Pockets
6 · best druggability 0.76

Structure

x-ray diffraction · 2 distinct chains · 23% helix, 29% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AGlucosidaseprotein47423% helix, 28% strandA0A1Z1FG87
BGlucosidaseprotein48323% helix, 30% strandA0A1Z1FG87

Ligands and binding sites

  • GOL · Glycerol · additive · 3 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13030.760.8850GOL
24890.730.8271empty
31260.440.7729empty
41270.430.7718empty
5550.320.7616empty

Interfaces

1 interface between chains.

  • A–B · 1084 Ų buried · 18 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 18 modified (engineered).

Compared structures

  • 5Z3K · Crystal structure of glucosidase from Croceicoccus marinus at 1.8 Angstrom resolution · the same entry in another collection · chain A against A, TM-score 1.00

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