3RT8: Chlorowillardiine

Chlorowillardiine bound to the ligand binding domain of GluA3. Determined by X-ray diffraction at 2.43 Å resolution. Released 18 May 2011.

Method
X-ray diffraction
Resolution
2.43 Å
Organism
Rattus norvegicus
Chains
1
Atoms
2,197
Mol. weight
29.26 kDa
Ligands
CWD, ZN
Released
18 May 2011

Explore 3RT8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3RT8 contains 15 α-helices and 20 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: 15 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand5-1061
β-strand1312
β-strand1712
β-strand18-1923
α-helix23-253
α-helix28-314
β-strand32-3323
α-helix35-4612
β-strand50-5561
β-strand6414
β-strand7114
α-helix73-797
β-strand85-8621
β-strand9115
α-helix94-974
β-strand100-10231
α-helix1031
α-helix1051
β-strand107-10935
β-strand111-11666
α-helix124-1285
β-strand134-13746
β-strand13817
α-helix142-1487
α-helix153-16311
β-strand17117
α-helix174-18310
β-strand188-19366
α-helix194-2007
β-strand208-21146
β-strand218-22035
β-strand223-22531
α-helix231-24313
α-helix246-2516
α-helix252-2565

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glutamate receptor 3Aprotein258Rattus norvegicusP19492 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3RT8_1 Glutamate receptor 3 (chains A)
RTIVVTTILESPYVMYKKNHEQLEGNERYEGYCVDLAYEIAKHVRIKYKLSIVGDGKYGA
RDPETKIWNGMVGELVYGRADIAVAPLTITLVREEVIDFSKPFMSLGISIMIKKGTPIES
AEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWSYMKSAEPSVFTKTTADGVARVRK
SKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSALGTPVNLAVLKLSE
QGILDKLKNKWWYDKGEC

Ligands and cofactors

IDNameFormulaCopies
CWD3-(5-chloro-2,4-dioxo-3,4-dihydropyrimidin-1(2H)-yl)-L-alanineC7 H8 Cl N3 O41
ZNZinc ionZn1

Primary citation

Mechanisms of Modal Activation of GluA3 Receptors. Poon, K., Ahmed, A.H., Nowak, L.M. et al. Mol Pharmacol (2011) 80:49-59. DOI 10.1124/mol.111.071688 · PubMed

Other PDB entries of the same protein (UniProt P19492 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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