4HV7
Structure of ricin A chain bound with N-(N-(pterin-7-yl)carbonylglycyl)glycine
Summary for 4HV7
| Entry DOI | 10.2210/pdb4hv7/pdb |
| Related | 1BR6 1IFT 1PX8 1PX9 1RTC 4ESI 4HV3 4huo 4hup |
| Descriptor | Ricin, 2-[2-[(2-azanyl-4-oxidanylidene-1H-pteridin-7-yl)carbonylamino]ethanoylamino]ethanoic acid, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | ricin, protein-ligand complex, pterin, hydrolase-hydrolase inhibitor complex, toxin, hydrolase, ribosome-inactivating protein, n-glycosidase, hydrolase/hydrolase inhibitor |
| Biological source | Ricinus communis (Castor bean) |
| Total number of polymer chains | 1 |
| Total formula weight | 30458.13 |
| Authors | Jasheway, K.R.,Monzingo, A.F.,Saito, R.,Pruet, J.M.,Manzano, L.A.,Wiget, P.A.,Anslyn, E.V.,Robertus, J.D. (deposition date: 2012-11-05, release date: 2012-12-26, Last modification date: 2023-09-20) |
| Primary citation | Saito, R.,Pruet, J.M.,Manzano, L.A.,Jasheway, K.,Monzingo, A.F.,Wiget, P.A.,Kamat, I.,Anslyn, E.V.,Robertus, J.D. Peptide-conjugated pterins as inhibitors of ricin toxin A. J.Med.Chem., 56:320-329, 2013 Cited by PubMed Abstract: Several 7-peptide-substituted pterins were synthesized and tested as competitive active-site inhibitors of ricin toxin A (RTA). Focus began on dipeptide conjugates, and these results further guided the construction of several tripeptide conjugates. The binding of these compounds to RTA was studied via a luminescence-based kinetic assay, as well as through X-ray crystallography. Despite the relatively polar, solvent exposed active site, several hydrophobic interactions, most commonly π-interactions not predicted by modeling programs, were identified in all of the best-performing inhibitors. Nearly all of these compounds provide IC₅₀ values in the low micromolar range. PubMed: 23214944DOI: 10.1021/jm3016393 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.869 Å) |
Structure validation
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