MolNFT v1 · #35921 · protein

N-acetyl-B-D-glucoasminidase (gcna) from stretococcus gordonii

2EPM · N-acetyl-beta-D-glucosaminidase: “N-acetyl-B-D-glucoasminidase (gcna) from stretococcus gordonii”. X-ray diffraction, 2 ligands (HG, SO4), 4 pockets (best druggability 0.55). MolNFT v1 #35921 on GenesisL1: 3D structure, binding…

PDB: 2EPM
Type: protein
Length: 592 residues
Chains: 1
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: HG, SO4
Pockets: 4 · best druggability 0.55

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	N-acetyl-beta-D-glucosaminidase (EC 3.2.1.52)	protein	592	49% helix, 14% strand	Q6ST21

Ligands and binding sites

HG · Mercury (II) ion · metal · 6 copies · chains X
SO4 · Sulfate ion · ion · 7 copies · chains X
GOL · Glycerol · additive · chains X

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	159	0.55	0.80	25	HG
2	214	0.45	0.73	26	empty
3	105	0.43	0.78	26	empty
4	57	0.36	0.79	14	empty

Compared structures

2EPM · N-acetyl-B-D-glucoasminidase (GCNA) from Stretococcus gordonii · the same entry in another collection · chain X against X, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt Q6ST21
Elsewhere: RCSB PDB 2EPM · PDBe 2EPM · UniProt Q6ST21

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