1HDK: Charcot-Leyden Crystal Protein - pCMBS Complex

Charcot-Leyden Crystal Protein - pCMBS Complex. Determined by X-ray diffraction at 1.8 Å resolution. Released 15 Nov 2001.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
HOMO SAPIENS
Chains
1
Atoms
1,232
Mol. weight
17.16 kDa
Ligands
PMB
Released
15 Nov 2001

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

Secondary structure: helices and β-sheets

1HDK contains 2 α-helices and 12 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: 2 helices, 12 β-strands

ElementResiduesLengthSheet
β-strand8-1141
β-strand19-2682
α-helix30-323
β-strand35-4171
β-strand50-5781
β-strand61-6881
β-strand71-7221
β-strand76-7831
β-strand89-9572
β-strand99-10462
β-strand107-11372
α-helix118-1203
β-strand123-12861
β-strand130-13782

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Eosinophil lysophospholipaseAprotein141HOMO SAPIENSQ05315 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1HDK_1 EOSINOPHIL LYSOPHOSPHOLIPASE (chains A)
SLLPVPYTEAASLSTGSTVTIKGRPLVCFLNEPYLQVDFHTEMKEESDIVFHFQVCFGRR
VVMNSREYGAWKQQVESKNMPFQDGQEFELSISVLPDKYQVMVNGQSSYTFDHRIKPEAV
KMVQVWRDISLTKFNVSYLKR

Ligands and cofactors

IDNameFormulaCopies
PMBPara-mercury-benzenesulfonic acidC6 H5 Cl Hg O3 S2

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. 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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