Research workbench

The structure of a family 25 glycosyl hydrolase from bacillus anthracis.

Analyse The structure of a family 25 glycosyl hydrolase from bacillus anthracis. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2WAG
Type: protein
Length: 217 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysozyme, putative
EC: 3.2.1.17
UniProt: Q81YN8
Ligands: MG, SO4
Pockets: 2 · best druggability 0.52

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 22% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysozyme, putative (EC 3.2.1.17)	protein	217	29% helix, 22% strand	Q81YN8

Ligands and binding sites

MG · Magnesium ion · metal · chains A
SO4 · Sulfate ion · ion · 5 copies · chains A
15P · Polyethylene glycol (N=34) · additive · 5 copies · 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

2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	86	0.52	0.84	15	GOL
2	116	0.41	0.76	21	empty

Compared structures

2WAG · The Structure of a family 25 Glycosyl hydrolase from Bacillus anthracis. · 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 Q81YN8
Elsewhere: RCSB PDB 2WAG · PDBe 2WAG · UniProt Q81YN8

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.