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Crystal structure of Streptococcus mutans dextran glucosidase

Analyse Crystal structure of Streptococcus mutans dextran glucosidase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2ZIC
Type: protein
Length: 536 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.2
Source: Streptococcus mutans
Molecule: Dextran glucosidase
EC: 3.2.1.70
UniProt: Q2HWU5
Ligands: CA
Pockets: 3 · best druggability 0.63

Structure

x-ray diffraction · resolution 2.2 · 1 distinct chain · 37% helix, 18% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Dextran glucosidase (EC 3.2.1.70)	protein	536	37% helix, 18% strand	Q2HWU5

Ligands and binding sites

CA · Calcium ion · metal · 3 copies · chains A
TRS · 2-amino-2-hydroxymethyl-propane-1,3-diol · additive · chains A
GOL · Glycerol · additive · chains A

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	334	0.63	0.79	39	TRS, GOL
2	146	0.58	0.83	23	empty
3	70	0.36	0.77	14	empty

Compared structures

2ZIC · Crystal structure of streptococcus mutans dextran glucosidase · 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 Q2HWU5
Elsewhere: RCSB PDB 2ZIC · PDBe 2ZIC · UniProt Q2HWU5

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