Crystal structure of Galectin-8 N-CRD with N-acetyllactosamine. Determined by X-ray diffraction at 1.75 Å resolution. Released 12 Nov 2025.
Explore 9KH4 in 3D Show helices and sheets RCSB PDB PDBe
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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 16-20 | 5 | 1 |
| α-helix | 22-23 | 2 | |
| β-strand | 26-29 | 4 | 2 |
| β-strand | 39-45 | 7 | 1 |
| β-strand | 52-59 | 8 | 2 |
| α-helix | 67 | 1 | |
| β-strand | 68-76 | 9 | 2 |
| β-strand | 82-89 | 8 | 2 |
| β-strand | 92-93 | 2 | 2 |
| β-strand | 97-99 | 3 | 2 |
| β-strand | 109-116 | 8 | 1 |
| β-strand | 120-125 | 6 | 1 |
| β-strand | 128-134 | 7 | 1 |
| α-helix | 139-141 | 3 | |
| β-strand | 144-149 | 6 | 2 |
| β-strand | 152-159 | 8 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Galectin-8 | A | protein | 150 | Homo sapiens | O00214 (AlphaFold model) |
>9KH4_1 Galectin-8 (chains A) SLNNLQNIIYNPVIPFVGTIPDQLDPGTLIVIRGHVPSDADRFQVDLQNGSSMKPRADVA FHFNPRFKRAGCIVCNTLINEKWGREEITYDTPFKREKSFEIVIMVLKDKFQVAVNGKHT LLYGHRIGPEKIDTLGIYGKVNIHSIGFSF
| ID | Name | Formula | Copies |
|---|---|---|---|
| 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 O11 | 1 |
| NI | Nickel (II) ion | Ni | 1 |
Water and common crystallization additives (NA) are not listed.
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:
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