1FQJ: PDB entry 1FQJ

Crystal structure of the heterotrimeric complex of the rgs domain of RGS9, the gamma subunit of phosphodiesterase and the GT/I1 chimera alpha subunit [(RGS9)-(pdegamma)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)]. Determined by X-ray diffraction at 2.02 Å resolution. Released 28 Feb 2001.

Method
X-ray diffraction
Resolution
2.02 Å
Organisms
Bos taurus, Rattus norvegicus
Chains
5
Atoms
8,107
Mol. weight
115.26 kDa
Ligands
MG, ALF, GDP
Released
28 Feb 2001

Explore 1FQJ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1FQJ contains 66 α-helices and 16 β-strands across 5 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: 19 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand29-3681
α-helix42-5312
α-helix59-635
α-helix66-8621
α-helix95-10915
α-helix1111
α-helix117-12711
α-helix130-1367
α-helix139-1413
α-helix148-1525
α-helix155-1584
α-helix167-1715
β-strand180-18781
β-strand190-19781
α-helix201-21010
β-strand216-22271
α-helix223-2275
β-strand22912
β-strand23712
α-helix238-25013
α-helix253-2553
β-strand259-26571
α-helix267-2737
α-helix279-2813
α-helix292-30413
β-strand316-31941
α-helix325-34218
Chain B: 11 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix290-2956
α-helix300-3045
α-helix307-31913
α-helix324-33714
α-helix343-3508
α-helix351-3555
α-helix367-37610
α-helix386-39510
α-helix396-4005
α-helix401-4066
α-helix408-4158
Chain C: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix621
α-helix63-675
α-helix69-735
α-helix78-836
Chain D: 19 helices, 8 β-strands
ElementResiduesLengthSheet
β-strand29-3683
α-helix42-5211
α-helix59-635
α-helix65-8622
α-helix95-10713
α-helix1111
α-helix117-12711
α-helix130-1367
α-helix139-1413
α-helix148-1525
α-helix155-1595
α-helix167-1726
β-strand180-18783
β-strand190-19783
α-helix201-21010
β-strand216-22273
α-helix223-2275
β-strand22914
β-strand23714
α-helix238-25013
β-strand259-26573
α-helix267-2748
α-helix279-2813
α-helix295-30410
α-helix308-3114
β-strand316-31943
α-helix325-34016
Chain E: 13 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix279-2813
α-helix290-2956
α-helix300-3045
α-helix307-31913
α-helix324-33714
α-helix340-3423
α-helix343-3508
α-helix351-3555
α-helix367-37610
α-helix386-39611
α-helix397-4015
α-helix402-4043
α-helix408-4158

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Guanine nucleotide-binding protein G(t) subunit alpha-1,Guanine nucleotide-binding protein G(i)…A, Dprotein325Bos taurus, Rattus norvegicusP04695 (AlphaFold model), P10824 (AlphaFold model)
Regulator of G-protein signaling 9B, Eprotein147Bos taurusO46469 (AlphaFold model)
Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gammaCprotein42Bos taurusP04972 (AlphaFold model)
Sequence of entity 1 (A, D), FASTA
>1FQJ_1 Guanine nucleotide-binding protein G(t) subunit alpha-1,Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(t) subunit alpha-1 (chains A, D)
DARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIVRAMT
TLNIQYGDSARQDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFDRASEYQLN
DSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERK
KWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLN
KKDLFEEKIKKSPLTICYPEYAGSNTYEEAGNYIKVQFLELNMRRDVKEIYSHMTCATDT
QNVKFVFDAVTDIIIKENLKDCGLF
Sequence of entity 2 (B, E), FASTA
>1FQJ_2 Regulator of G-protein signaling 9 (chains B, E)
QFWDLNAKLVDIPTKMRVERWAFNFSELIRDPKGRQSFQHFLRKEFSGENLGFWEACEDL
KYGDQSKVKEKAEEIYKLFLAPGARRWINIDGKTMDITVKGLKHPHRYVLDAAQTHIYML
MKKDSYARYLKSPIYKEMLAKAIEPQG
Sequence of entity 3 (C), FASTA
>1FQJ_3 Retinal rod rhodopsin-sensitive cGMP 3',5'-cyclic phosphodiesterase subunit gamma (chains C)
GVQGFGDDIPGMEGLGTDITVICPWEAFNHLELHELAQYGII

Ligands and cofactors

IDNameFormulaCopies
MGMagnesium ionMg2
ALFTetrafluoroaluminate ionAl F42
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P22

Primary citation

Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A. Slep, K.C., Kercher, M.A., He, W. et al. Nature (2001) 409:1071-1077. DOI 10.1038/35059138 · PubMed

Other PDB entries of the same protein (UniProt P04695 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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