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The crystal structure of 6-phospho-beta-glucosidase mutant (E375Q) in complex with salicin 6-phosphate

Analyse The crystal structure of 6-phospho-beta-glucosidase mutant (E375Q) in complex… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4F79
Type: protein
Length: 478 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Putative phospho-beta-glucosidase
EC: 3.2.1.86
UniProt: Q8DT00
Ligands: P53
Pockets: 1 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 41% helix, 15% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Putative phospho-beta-glucosidase (EC 3.2.1.86)	protein	478	41% helix, 15% strand	Q8DT00

Ligands and binding sites

P53 · 2-(hydroxymethyl)phenyl 6-O-phosphono-beta-D-glucopyranoside · ligand · chains A
GOL · Glycerol · additive · 2 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	632	0.75	0.81	50	P53

Compared structures

4F79 · The crystal structure of 6-phospho-beta-glucosidase mutant (E375Q) in complex with… · 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 Q8DT00
Elsewhere: RCSB PDB 4F79 · PDBe 4F79 · UniProt Q8DT00

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