1G86: Charcot-leyden crystal protein

Charcot-leyden crystal protein/n-ethylmaleimide complex. Determined by X-ray diffraction at 1.8 Å resolution. Released 19 Jun 2002.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Homo sapiens
Chains
1
Atoms
1,245
Mol. weight
16.75 kDa
Ligands
NEQ
Released
19 Jun 2002

Explore 1G86 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1G86 contains 3 α-helices and 13 β-strands across 1 chain. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.

Chain A: 3 helices, 13 β-strands

ElementResiduesLengthSheet
β-strand411
β-strand8-1142
β-strand19-2681
α-helix30-323
β-strand35-4172
β-strand50-5782
β-strand61-6882
β-strand71-7222
β-strand76-7832
α-helix83-842
β-strand89-9571
β-strand99-10461
β-strand107-11371
α-helix118-1203
β-strand123-12862
β-strand130-13781

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Charcot-leyden crystal proteinAprotein142Homo sapiensQ05315 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1G86_1 CHARCOT-LEYDEN CRYSTAL PROTEIN (chains A)
MSLLPVPYTEAASLSTGSTVTIKGRPLVCFLNEPYLQVDFHTEMKEESDIVFHFQVCFGR
RVVMNSREYGAWKQQVESKNMPFQDGQEFELSISVLPDKYQVMVNGQSSYTFDHRIKPEA
VKMVQVWRDISLTKFNVSYLKR

Ligands and cofactors

IDNameFormulaCopies
NEQN-ethylmaleimideC6 H7 N O22

Primary citation

Charcot-Leyden crystal protein (galectin-10) is not a dual function galectin with lysophospholipase activity but binds a lysophospholipase inhibitor in a novel structural fashion. Ackerman, S.J., Liu, L., Kwatia, M.A. et al. J Biol Chem (2002) 277:14859-14868. DOI 10.1074/jbc.M200221200 · PubMed

Other PDB entries of the same protein (UniProt Q05315 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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