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Crystal structure of streptococcus agalactiae beta-glucuronidase in space group I222

Analyse Crystal structure of streptococcus agalactiae beta-glucuronidase in space group… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4JKK
Type
protein
Length
588 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-glucuronidase
EC
3.2.1.31
UniProt
Q8E0N2
Ligands
MG
Pockets
5 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 18% helix, 35% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ABeta-glucuronidase (EC 3.2.1.31)protein58818% helix, 35% strandQ8E0N2

Ligands and binding sites

  • MG · Magnesium ion · metal · chains A

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
13780.650.7933empty
2840.510.8425empty
31650.510.7823empty
41280.480.7818empty
5760.460.8218empty

Compared structures

  • 4JKK · Crystal Structure of Streptococcus agalactiae beta-glucuronidase in space group I222 · the same entry in another collection · chain A against A, TM-score 1.00

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