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Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain E148A mutant in complex with a(GlcNAc)2

Analyse Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3WL0
Type: protein
Length: 383 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.204
Source: Ostrinia furnacalis
Molecule: Chitinase
EC: 3.2.1.14
UniProt: Q2V6H4
Ligands: NAG
Pockets: 2 · best druggability 0.68

Structure

x-ray diffraction · resolution 2.204 · 1 distinct chain · 39% helix, 21% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chitinase (EC 3.2.1.14)	protein	383	39% helix, 21% strand	Q2V6H4

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 4 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	410	0.68	0.80	48	NAG
2	50	0.35	0.79	17	empty

Modifications

Observed in the structure: 3 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

3WL0 · Crystal structure of ostrinia furnacalis group I chitinase catalytic domain E148A mutant… · 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 Q2V6H4
Elsewhere: RCSB PDB 3WL0 · PDBe 3WL0 · UniProt Q2V6H4

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