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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: 2EPK
Type: protein
Length: 613 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: SO4
Pockets: 5 · best druggability 0.49

Structure

x-ray diffraction · 1 distinct chain · 50% helix, 13% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
X	N-acetyl-beta-D-glucosaminidase (EC 3.2.1.52)	protein	613	50% helix, 13% strand	Q6ST21

Ligands and binding sites

SO4 · Sulfate ion · ion · 7 copies · chains X

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

Pockets

5 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	174	0.49	0.76	26	empty
2	199	0.44	0.73	24	empty
3	54	0.40	0.82	15	empty
4	53	0.38	0.81	13	empty
5	57	0.28	0.74	16	empty

Modifications

Observed in the structure: 14 modified (engineered).

Compared structures

2EPK · N-acetyl-B-D-glucosaminidase (GCNA) from Streptococcus 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 2EPK · PDBe 2EPK · UniProt Q6ST21

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