Research workbench

Charcot-leyden crystal protein

Analyse Charcot-leyden crystal protein in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1LCL
Type: protein
Length: 141 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Lysophospholipase
EC: 3.1.1.5
UniProt: Q05315

Structure

x-ray diffraction · 1 distinct chain · 4% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Lysophospholipase (EC 3.1.1.5)	protein	141	4% helix, 53% strand	Q05315

Compared structures

1LCL · Charcot-leyden crystal protein · the same entry in another collection · chain A against A, TM-score 1.00
Q05315 · AlphaFold monomer V2.0 prediction for galectin-10 (Q05315) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q05315
Elsewhere: RCSB PDB 1LCL · PDBe 1LCL · UniProt Q05315

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.