3FAS: IGluR4 flip ligand-binding core

X-ray structure of iGluR4 flip ligand-binding core (S1S2) in complex with (S)-glutamate at 1.40A resolution. Determined by X-ray diffraction at 1.4 Å resolution. Released 9 Dec 2008.

Method
X-ray diffraction
Resolution
1.4 Å
Organism
Rattus norvegicus
Chains
2
Atoms
5,287
Mol. weight
59.93 kDa
Ligands
GLU
Released
9 Dec 2008

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

Secondary structure: helices and β-sheets

3FAS contains 32 α-helices and 40 β-strands across 2 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.

Chain A: 16 helices, 20 β-strands

ElementResiduesLengthSheet
β-strand3-861
β-strand1112
β-strand1512
β-strand16-1723
α-helix181
α-helix21-233
α-helix26-294
β-strand30-3123
α-helix33-4513
β-strand48-5361
β-strand6214
β-strand6914
α-helix71-777
β-strand83-8421
β-strand8915
α-helix92-954
β-strand98-10031
α-helix1011
α-helix1031
β-strand105-10735
β-strand109-11466
α-helix122-1265
β-strand132-13436
β-strand13617
α-helix140-1478
α-helix151-16111
β-strand16917
α-helix172-18110
β-strand186-19166
α-helix192-1998
β-strand206-20946
β-strand216-21835
β-strand221-22331
α-helix229-24113
α-helix244-2496
α-helix250-2545
Chain B: 16 helices, 20 β-strands
ElementResiduesLengthSheet
β-strand3-868
β-strand1119
β-strand1519
β-strand16-17210
α-helix181
α-helix21-233
α-helix26-294
β-strand30-31210
α-helix33-4513
β-strand48-5368
β-strand62111
β-strand69111
α-helix71-777
β-strand83-8428
β-strand89112
α-helix92-954
β-strand98-10038
α-helix1011
α-helix1031
β-strand105-107312
β-strand109-114613
α-helix122-1265
β-strand132-134313
β-strand135-136214
α-helix140-1478
α-helix151-16111
β-strand168-169214
α-helix172-18110
β-strand186-191613
α-helix192-1987
β-strand206-209413
β-strand216-218312
β-strand221-22338
α-helix229-24113
α-helix244-2496
α-helix250-2545

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Glutamate receptor 4A, Bprotein260Rattus norvegicusP19493 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3FAS_1 Glutamate receptor 4 (chains A, B)
GRTVVVTTIMESPYVMYKKNHEMFEGNDKYEGYCVDLASEIAKHIGIKYKIAIVPDGKYG
ARDADTKIWNGMVGELVYGKAEIAIAPLTITLVREEVIDFSKPFMSLGISIMIKKGTPIE
SAEDLAKQTEIAYGTLDSGSTKEFFRRSKIAVYEKMWTYMRSAEPSVFTRTTAEGVARVR
KSKGKFAFLLESTMNEYIEQRKPCDTMKVGGNLDSKGYGVATPKGSSLRTPVNLAVLKLS
EAGVLDKLKNKWWYDKGECG

Ligands and cofactors

IDNameFormulaCopies
GLUGlutamic acidC5 H9 N O42

Water and common crystallization additives (SO4, GOL) are not listed.

Primary citation

Molecular mechanism of agonist recognition by the ligand-binding core of the ionotropic glutamate receptor 4. Kasper, C., Frydenvang, K., Naur, P. et al. FEBS Lett (2008) 582:4089-4094. DOI 10.1016/j.febslet.2008.11.005 · PubMed

Other PDB entries of the same protein (UniProt P19493 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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