Fundamental Characterization of Chelated and Crystallized Actinium in a Macromolecular Host. Determined by X-ray diffraction at 2.08 Å resolution. Released 25 Sept 2024.
Explore 8UZ9 in 3D Show helices and sheets RCSB PDB PDBe
8UZ9 contains 31 α-helices and 33 β-strands across 3 chains. 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 |
|---|---|---|---|
| α-helix | 8-12 | 5 | |
| α-helix | 13-15 | 3 | |
| β-strand | 29-38 | 10 | 1 |
| α-helix | 48-49 | 2 | |
| β-strand | 50 | 1 | 2 |
| α-helix | 51 | 1 | |
| β-strand | 53-58 | 6 | 1 |
| α-helix | 63 | 1 | |
| β-strand | 64-72 | 9 | 1 |
| β-strand | 75-85 | 11 | 1 |
| β-strand | 91-94 | 4 | 1 |
| α-helix | 97-99 | 3 | |
| β-strand | 103-113 | 11 | 1 |
| β-strand | 118-127 | 10 | 1 |
| β-strand | 130-139 | 10 | 1 |
| α-helix | 146-158 | 13 | |
| α-helix | 163-165 | 3 | |
| β-strand | 166-167 | 2 | 1 |
| α-helix | 169 | 1 | |
| β-strand | 170 | 1 | 2 |
| α-helix | 171 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-12 | 5 | |
| α-helix | 13-15 | 3 | |
| α-helix | 24-27 | 4 | |
| β-strand | 29-38 | 10 | 3 |
| α-helix | 49 | 1 | |
| β-strand | 50 | 1 | 4 |
| α-helix | 51 | 1 | |
| β-strand | 53-58 | 6 | 3 |
| α-helix | 63 | 1 | |
| β-strand | 64-72 | 9 | 3 |
| β-strand | 75-85 | 11 | 3 |
| β-strand | 91-94 | 4 | 3 |
| α-helix | 97-99 | 3 | |
| β-strand | 103-113 | 11 | 3 |
| β-strand | 118-127 | 10 | 3 |
| β-strand | 130-139 | 10 | 3 |
| α-helix | 146-158 | 13 | |
| α-helix | 163-165 | 3 | |
| β-strand | 166-167 | 2 | 3 |
| α-helix | 169 | 1 | |
| β-strand | 170 | 1 | 4 |
| α-helix | 171 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Neutrophil gelatinase-associated lipocalin | A, B, C | protein | 178 | Homo sapiens | P80188 (AlphaFold model) |
>8UZ9_1 Neutrophil gelatinase-associated lipocalin (chains A, B, C) QDSTSDLIPAPPLSKVPLQQNFQDNQFQGKWYVVGLAGNAILREDKDPQKMYATIYELKE DKSYNVTSVLFRKKKCDYWIRTFVPGSQPGEFTLGNIKSYPGLTSYLVRVVSTNYNQHAM VFFKKVSQNREYFKITLYGRTKELTSELKENFIRFSKSLGLPENHIVFPVPIDQCIDG
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZTM | Actinium Ion | Ac | 3 |
| 4OL | N,N'-butane-1,4-diylbis[1-hydroxy-N-(3-{[(1-hydroxy-6-oxo-1,6-dihydropyridin-2-… | C34 H38 N8 O12 | 3 |
Water and common crystallization additives (CL, SO4) are not listed.
Actinium chelation and crystallization in a macromolecular scaffold. Wacker, J.N., Woods, J.J., Rupert, P.B. et al. Nat Commun (2024) 15:5741-5741. DOI 10.1038/s41467-024-50017-5 · PubMed
Other PDB entries of the same protein (UniProt P80188 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 8UZ9 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.