MolNFT v1 · #19451 · protein

Charcot-leyden crystal protein - mannose complex

1QKQ · Eosinophil lysophospholipase: “Charcot-leyden crystal protein - mannose complex”. X-ray diffraction, 1 ligand (MAN). MolNFT v1 #19451 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

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

Structure

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

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

Ligands and binding sites

MAN · alpha-D-mannopyranose · sugar · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Compared structures

1QKQ · Charcot-leyden crystal protein - mannose complex · 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 1QKQ · PDBe 1QKQ · UniProt Q05315

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