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Crystal structure of unsaturated glucuronyl hydrolase mutant D115N/K370S from streptococcus agalactiae

Analyse Crystal structure of unsaturated glucuronyl hydrolase mutant D115N/K370S from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WUX
Type: protein
Length: 376 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Unsaturated chondroitin disaccharide hydrolase
EC: 3.2.1.180
UniProt: Q8E372
Pockets: 1 · best druggability 0.73

Structure

x-ray diffraction · 1 distinct chain · 55% helix, 7% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Unsaturated chondroitin disaccharide hydrolase (EC 3.2.1.180)	protein	376	55% helix, 7% strand	Q8E372

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 12 copies · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	466	0.73	0.83	51	EDO

Compared structures

3WUX · Crystal structure of unsaturated glucuronyl hydrolase mutant D115N/K370S from… · the same entry in another collection · chain A against A, TM-score 1.00
Q8E372 · AlphaFold monomer V2.0 prediction for unsaturated chondroitin disaccharide hydrolase… · a predicted model of the same protein · chain A against A, TM-score 0.96

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 Q8E372
Elsewhere: RCSB PDB 3WUX · PDBe 3WUX · UniProt Q8E372

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