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Structure and activity of the GH20 beta-N- acetylhexosaminidase from streptomyces coelicolor A3(2)

Analyse Structure and activity of the GH20 beta-N- acetylhexosaminidase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4C7G
Type: protein
Length: 494 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-N-acetylhexosaminidase
EC: 3.2.1.52
UniProt: Q9L068
Ligands: NGO
Pockets: 2 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-N-acetylhexosaminidase (EC 3.2.1.52)	protein	494	36% helix, 17% strand	Q9L068

Ligands and binding sites

NGO · 2-methyl-4,5-dihydro-(1,2-dideoxy-alpha-D-glucopyranoso)[2,1-D]-1,3-oxazole · ligand · chains A
EDO · 1,2-ethanediol · additive · 11 copies · chains A

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

Pockets

2 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	73	0.51	0.84	17	NGO, EDO
2	135	0.41	0.75	19	empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

4C7G · Structure and activity of the GH20 beta-N-acetylhexosaminidase from Streptomyces… · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt Q9L068
Elsewhere: RCSB PDB 4C7G · PDBe 4C7G · UniProt Q9L068

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