9KH4: Galectin-8 N-CRD with N-acetyllactosamine

Crystal structure of Galectin-8 N-CRD with N-acetyllactosamine. Determined by X-ray diffraction at 1.75 Å resolution. Released 12 Nov 2025.

Method
X-ray diffraction
Resolution
1.75 Å
Organism
Homo sapiens
Chains
1
Atoms
1,426
Mol. weight
17.46 kDa
Ligands
RNQ, NI
Released
12 Nov 2025

Explore 9KH4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9KH4 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-strand16-2051
α-helix22-232
β-strand26-2942
β-strand39-4571
β-strand52-5982
α-helix671
β-strand68-7692
β-strand82-8982
β-strand92-9322
β-strand97-9932
β-strand109-11681
β-strand120-12561
β-strand128-13471
α-helix139-1413
β-strand144-14962
β-strand152-15981

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Galectin-8Aprotein150Homo sapiensO00214 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9KH4_1 Galectin-8 (chains A)
SLNNLQNIIYNPVIPFVGTIPDQLDPGTLIVIRGHVPSDADRFQVDLQNGSSMKPRADVA
FHFNPRFKRAGCIVCNTLINEKWGREEITYDTPFKREKSFEIVIMVLKDKFQVAVNGKHT
LLYGHRIGPEKIDTLGIYGKVNIHSIGFSF

Ligands and cofactors

IDNameFormulaCopies
RNQ~{N}-[(2~{R},3~{R},4~{R},5~{S},6~{R})-6-(hydroxymethyl)-5-[(2~{S},3~{R},4~{S},5…C14 H25 N O111
NINickel (II) ionNi1

Water and common crystallization additives (NA) are not listed.

Primary citation

Galectin-8 binding to alpha-1 antitrypsin is a physiological mechanism in healthy individuals but exacerbates the symptoms of alpha-1 antitrypsin deficiency. Sayed, H., Mayo, K.H., Zhou, Y. et al. Arch Biochem Biophys (2025) 772:110577-110577. DOI 10.1016/j.abb.2025.110577 · PubMed

Other PDB entries of the same protein (UniProt O00214 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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