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Crystal structure of class V chitinase (E115Q mutant) from nicotiana tobaccum in complex with NAG4

Analyse Crystal structure of class V chitinase (E115Q mutant) from nicotiana tobaccum… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3ALG
Type: protein
Length: 348 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chitinase, class V
EC: 3.2.1.14
UniProt: Q43576
Ligands: NAG, PO4
Pockets: 1 · best druggability 0.58

Structure

x-ray diffraction · 1 distinct chain · 39% helix, 26% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chitinase, class V (EC 3.2.1.14)	protein	348	39% helix, 26% strand	Q43576

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 copies · chains A
PO4 · Phosphate ion · ion · 3 copies · chains A
EDO · 1,2-ethanediol · additive · 8 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	371	0.58	0.75	49	NAG, EDO

Compared structures

3ALG · Crystal Structure of Class V Chitinase (E115Q mutant) from Nicotiana tobaccum in complex… · 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 Q43576
Elsewhere: RCSB PDB 3ALG · PDBe 3ALG · UniProt Q43576

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