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N-acetyl-B-D-glucosaminidase (gcna) from streptococcus gordonii

Analyse N-acetyl-B-D-glucosaminidase (gcna) from streptococcus gordonii in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2EPN
Type
protein
Length
1,246 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
N-acetyl-beta-D-glucosaminidase
EC
3.2.1.52
UniProt
Q6ST21
Ligands
NGT
Pockets
10 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 51% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BN-acetyl-beta-D-glucosaminidase (EC 3.2.1.52)protein62351% helix, 13% strandQ6ST21

Ligands and binding sites

  • NGT · 3ar,5r,6s,7r,7ar-5-hydroxymethyl-2-methyl-5,6,7,7A-tetrahydro-3AH-pyrano[3,2-d]thiazole-6,7-diol · ligand · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13230.650.8046empty
22050.630.8233NGT
32050.620.8232NGT
42230.600.8135empty
51090.490.8019empty

Interfaces

1 interface between chains.

  • A–B · 3705 Ų buried · 52 hydrogen bonds · protein-protein

Compared structures

  • 2EPN · N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus gordonii · the same entry in another collection · chain A against A, TM-score 1.00

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