8UYN

Fundamental Characterization of Chelated and Crystallized Actinium in a Macromolecular Host


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.205 

Starting Model: experimental
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Ligand Structure Quality Assessment 


This is version 1.1 of the entry. See complete history


Literature

Actinium chelation and crystallization in a macromolecular scaffold.

Wacker, J.N.Woods, J.J.Rupert, P.B.Peterson, A.Allaire, M.Lukens, W.W.Gaiser, A.N.Minasian, S.G.Strong, R.K.Abergel, R.J.

(2024) Nat Commun 15: 5741-5741

  • DOI: https://doi.org/10.1038/s41467-024-50017-5
  • Primary Citation of Related Structures:  
    8UYN, 8UZ9

  • PubMed Abstract: 

    Targeted alpha therapy (TAT) pairs the specificity of antigen targeting with the lethality of alpha particles to eradicate cancerous cells. Actinium-225 [ 225 Ac; t 1/2  = 9.920(3) days] is an alpha-emitting radioisotope driving the next generation of TAT radiopharmaceuticals. Despite promising clinical results, a fundamental understanding of Ac coordination chemistry lags behind the rest of the Periodic Table due to its limited availability, lack of stable isotopes, and inadequate systems poised to probe the chemical behavior of this radionuclide. In this work, we demonstrate a platform that combines an 8-coordinate synthetic ligand and a mammalian protein to characterize the solution and solid-state behavior of the longest-lived Ac isotope, 227 Ac [t 1/2  = 21.772(3) years]. We expect these results to direct renewed efforts for 225 Ac-TAT development, aid in understanding Ac coordination behavior relative to other +3 lanthanides and actinides, and more broadly inform this element's position on the Periodic Table.


  • Organizational Affiliation

    Chemical Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, CA, 94720, USA.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Neutrophil gelatinase-associated lipocalin
A, B, C
178Homo sapiensMutation(s): 0 
Gene Names: LCN2
UniProt & NIH Common Fund Data Resources
Find proteins for P80188 (Homo sapiens)
Explore P80188 
Go to UniProtKB:  P80188
PHAROS:  P80188
GTEx:  ENSG00000148346 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP80188
Sequence Annotations
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  • Reference Sequence
Small Molecules
Ligands 4 Unique
IDChains Name / Formula / InChI Key2D Diagram3D Interactions
4OL (Subject of Investigation/LOI)
Query on 4OL

Download Ideal Coordinates CCD File 
E [auth A],
G [auth B],
K [auth C]
N,N'-butane-1,4-diylbis[1-hydroxy-N-(3-{[(1-hydroxy-6-oxo-1,6-dihydropyridin-2-yl)carbonyl]amino}propyl)-6-oxo-1,6-dihydropyridine-2-carboxamide]
C34 H38 N8 O12
KUWKQASGHNTJAT-UHFFFAOYSA-N
PIN (Subject of Investigation/LOI)
Query on PIN

Download Ideal Coordinates CCD File 
I [auth C]PIPERAZINE-N,N'-BIS(2-ETHANESULFONIC ACID)
C8 H18 N2 O6 S2
IHPYMWDTONKSCO-UHFFFAOYSA-N
LA
Query on LA

Download Ideal Coordinates CCD File 
D [auth A],
F [auth B],
J [auth C]
LANTHANUM (III) ION
La
CZMAIROVPAYCMU-UHFFFAOYSA-N
SO4
Query on SO4

Download Ideal Coordinates CCD File 
H [auth B]SULFATE ION
O4 S
QAOWNCQODCNURD-UHFFFAOYSA-L
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.00 Å
  • R-Value Free: 0.227 
  • R-Value Work: 0.204 
  • R-Value Observed: 0.205 
  • Space Group: P 41 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 116.148α = 90
b = 116.148β = 90
c = 117.562γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
SCALEPACKdata scaling
DENZOdata reduction
REFMACphasing

Structure Validation

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Ligand Structure Quality Assessment 


Entry History & Funding Information

Deposition Data


Funding OrganizationLocationGrant Number
Not funded--

Revision History  (Full details and data files)

  • Version 1.0: 2024-09-25
    Type: Initial release
  • Version 1.1: 2024-11-20
    Changes: Structure summary