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Crystal structure of human chitotriosidase at 2.2 ångström resolution

Analyse Crystal structure of human chitotriosidase at 2.2 ångström resolution in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LQ0
Type: protein
Length: 365 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Chitotriosidase
UniProt: Q13231
Pockets: 1 · best druggability 0.63

Structure

x-ray diffraction · 1 distinct chain · 36% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Chitotriosidase	protein	365	36% helix, 23% strand	Q13231

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	387	0.63	0.77	44	empty

Modifications

Observed in the structure: 2 disulfide (disulfide).

Compared structures

1LQ0 · Crystal structure of human chitotriosidase at 2.2 ångström resolution · 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 0.99

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 1LQ0 · PDBe 1LQ0 · UniProt Q13231

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