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Inactive D62N mutant of BT1760 Endo-acting levanase from Bacteroides thetaiotaomicron VPI-5482

Analyse Inactive D62N mutant of BT1760 Endo-acting levanase from Bacteroides… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7ZNS
Type: protein
Length: 974 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.3
Source: Bacteroides thetaiotaomicron VPI-5482
Molecule: Glycoside hydrolase family 32
UniProt: Q8A6W6
Ligands: FRU, SO4
Pockets: 6 · best druggability 0.60

Structure

x-ray diffraction · resolution 2.3 · 1 distinct chain · 5% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Glycoside hydrolase family 32	protein	487	5% helix, 50% strand	Q8A6W6

Ligands and binding sites

FRU · beta-D-fructofuranose · sugar · 11 copies · chains A, B
SO4 · Sulfate ion · ion · 21 copies · chains A, B

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

Pockets

6 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	263	0.60	0.79	26	empty
2	252	0.59	0.79	27	empty
3	179	0.50	0.77	29	FRU
4	169	0.48	0.77	29	FRU
5	58	0.30	0.75	16	empty

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 Q8A6W6
Elsewhere: RCSB PDB 7ZNS · PDBe 7ZNS · UniProt Q8A6W6

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