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Crystal structure of endoglycosidase E GH20 domain from enterococcus faecalis

Analyse Crystal structure of endoglycosidase E GH20 domain from enterococcus faecalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7PUL
Type: protein
Length: 352 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Beta-N-acetylhexosaminidase; Gly-ala-gly-ala-ala
EC: 3.2.1.52
UniProt: Q6U890
Ligands: MG, CA
Pockets: 1 · best druggability 0.47

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-N-acetylhexosaminidase (EC 3.2.1.52)	protein	347	38% helix, 18% strand	Q6U890
P	Gly-ala-gly-ala-ala	protein	5	0% helix, 0% strand	—

Ligands and binding sites

MG · Magnesium ion · metal · 3 copies · chains A
CA · Calcium ion · metal · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	103	0.47	0.80	18	empty

Interfaces

1 interface between chains.

A–P · 103 Å² buried · 2 hydrogen bonds · protein-protein

Compared structures

7PUL · Crystal structure of Endoglycosidase E GH20 domain from Enterococcus faecalis · 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 Q6U890
Elsewhere: RCSB PDB 7PUL · PDBe 7PUL · UniProt Q6U890

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