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Crystal structure of endos, an endo-beta-N-acetyl-glucosaminidase from streptococcus pyogenes

Analyse Crystal structure of endos, an endo-beta-N-acetyl-glucosaminidase from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4NUY
Type: protein
Length: 880 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Endo-beta-N-acetylglucosaminidase F2
EC: 3.2.1.96
UniProt: Q48WW7
Ligands: CA
Pockets: 7 · best druggability 0.56

Structure

x-ray diffraction · 1 distinct chain · 28% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Endo-beta-N-acetylglucosaminidase F2 (EC 3.2.1.96)	protein	880	28% helix, 23% strand	Q48WW7

Ligands and binding sites

CA · Calcium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	244	0.56	0.78	38	empty
2	229	0.51	0.75	33	empty
3	170	0.50	0.78	33	empty
4	129	0.43	0.76	18	empty
5	54	0.40	0.80	9	empty

Compared structures

4NUY · Crystal structure of EndoS, an endo-beta-N-acetyl-glucosaminidase from Streptococcus… · the same entry in another collection · chain A against A, 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 Q48WW7
Elsewhere: RCSB PDB 4NUY · PDBe 4NUY · UniProt Q48WW7

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