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Crystal structure of human chitotriosidase in complex with ethylene glycol

Analyse Crystal structure of human chitotriosidase in complex with ethylene glycol in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LG2
Type: protein
Length: 359 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chitotriosidase
UniProt: Q13231
Pockets: 1 · best druggability 0.68

Structure

x-ray diffraction · 1 distinct chain · 35% helix, 24% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chitotriosidase	protein	359	35% helix, 24% strand	Q13231

Ligands and binding sites

EDO · 1,2-ethanediol · additive · 5 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	384	0.68	0.81	41	EDO

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1LG2 · Crystal structure of human chitotriosidase in complex with ethylene glycol · the same entry in another collection · chain A against A, TM-score 1.00
Q13231 · AlphaFold monomer V2.0 prediction for chitotriosidase-1 (Q13231) · a predicted model of the same protein · 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 Q13231
Elsewhere: RCSB PDB 1LG2 · PDBe 1LG2 · UniProt Q13231

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