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Crystal structures of MeBglD2 in complex with various saccharides

Analyse Crystal structures of MeBglD2 in complex with various saccharides in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7WDR
Type: protein
Length: 445 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2
Source: metagenome
Molecule: Beta-glucosidase
EC: 3.2.1.21
UniProt: A0A1E1FFN6
Ligands: PNW, SO4
Pockets: 1 · best druggability 0.74

Structure

x-ray diffraction · resolution 2 · 1 distinct chain · 44% helix, 17% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Beta-glucosidase (EC 3.2.1.21)	protein	445	44% helix, 17% strand	A0A1E1FFN6

Ligands and binding sites

PNW · 4-nitrophenyl beta-D-glucopyranoside · sugar · 2 copies · chains A
SO4 · Sulfate ion · ion · 3 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	521	0.74	0.82	43	PNW

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 A0A1E1FFN6
Elsewhere: RCSB PDB 7WDR · PDBe 7WDR · UniProt A0A1E1FFN6

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