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Crystal structure of ostrinia furnacalis group I chitinase catalytic domain in complex with reaction products (GLCNAC)2,3

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

PDB: 3WL1
Type: protein
Length: 383 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chitinase
EC: 3.2.1.14
UniProt: Q2V6H4
Ligands: NAG
Pockets: 1 · best druggability 0.66

Structure

x-ray diffraction · 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 · 7 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	402	0.66	0.79	50	NAG

Modifications

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

Compared structures

3WL1 · Crystal structure of Ostrinia furnacalis Group I chitinase catalytic domain 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 Q2V6H4
Elsewhere: RCSB PDB 3WL1 · PDBe 3WL1 · UniProt Q2V6H4

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