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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
2EPO
Type
protein
Length
1,227 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
Pockets
13 · best druggability 0.69

Structure

x-ray diffraction · 2 distinct chains · 50% helix, 13% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AN-acetyl-beta-D-glucosaminidase (EC 3.2.1.52)protein62650% helix, 12% strandQ6ST21
BN-acetyl-beta-D-glucosaminidase (EC 3.2.1.52)protein60150% helix, 13% strandQ6ST21

Ligands and binding sites

  • ACY · Acetic acid · additive · 2 copies · chains A, B

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
13510.690.8256empty
21080.530.8221ACY
31370.510.8023empty
4700.500.8414ACY
51060.500.8123empty

Interfaces

1 interface between chains.

  • A–B · 3577 Ų buried · 53 hydrogen bonds · protein-protein

Compared structures

  • 2EPO · 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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