1FQK: PDB entry 1FQK

Crystal structure of the heterodimeric complex of the rgs domain of RGS9, and the GT/I1 chimera alpha subunit [(RGS9)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)]. Determined by X-ray diffraction at 2.3 Å resolution. Released 28 Feb 2001.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: Bos taurus, Rattus norvegicus
Chains: 4
Atoms: 7,634
Mol. weight: 110.7 kDa
Ligands: GDP, ALF, MG
Released: 28 Feb 2001

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

Secondary structure: helices and β-sheets

1FQK contains 62 α-helices and 20 β-strands across 4 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: 20 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	29-36	8	1
α-helix	42-53	12
α-helix	59-63	5
α-helix	66-86	21
α-helix	96-109	14
α-helix	111	1
α-helix	117-127	11
α-helix	130-136	7
α-helix	139-141	3
α-helix	148-152	5
α-helix	155-158	4
α-helix	167-172	6
β-strand	180-187	8	1
β-strand	190-197	8	1
α-helix	201-204	4
α-helix	207-210	4
β-strand	216-222	7	1
α-helix	223-227	5
β-strand	229	1	2
β-strand	237	1	2
α-helix	238-250	13
α-helix	253-255	3
β-strand	259-265	7	1
α-helix	267-273	7
α-helix	279-281	3
α-helix	292-304	13
β-strand	316-320	5	1
α-helix	325-343	19

Chain B: 13 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	289	1	3
α-helix	290-294	5
α-helix	295-297	3
α-helix	300-304	5
α-helix	307-319	13
α-helix	324-336	13
α-helix	340-342	3
α-helix	343-350	8
α-helix	351-355	5
α-helix	367-376	10
α-helix	386-395	10
α-helix	396-401	6
α-helix	402-404	3
α-helix	408-415	8
β-strand	418	1	3

Chain C: 18 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	30-35	6	4
α-helix	42-52	11
α-helix	59-62	4
α-helix	65-86	22
α-helix	95-109	15
α-helix	117-127	11
α-helix	130-136	7
α-helix	139-141	3
α-helix	148-152	5
α-helix	155-158	4
α-helix	167-172	6
β-strand	180-187	8	4
β-strand	190-197	8	4
α-helix	201-207	7
α-helix	208-210	3
β-strand	216-222	7	4
α-helix	223-227	5
β-strand	229	1	5
β-strand	237	1	5
α-helix	238-250	13
β-strand	259-265	7	4
α-helix	267-276	10
α-helix	279-281	3
α-helix	292-304	13
β-strand	316-319	4	4
α-helix	325-340	16

Chain D: 11 helices, 2 β-strands

Element	Residues	Length	Sheet
β-strand	289	1	6
α-helix	290-298	9
α-helix	300-304	5
α-helix	307-319	13
α-helix	323-336	14
α-helix	343-350	8
α-helix	351-355	5
α-helix	367-376	10
α-helix	386-395	10
α-helix	396-401	6
α-helix	402-405	4
α-helix	408-414	7
β-strand	418	1	6

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanine nucleotide-binding protein G(t) subunit alpha-1,Guanine nucleotide-binding protein G(i)…	A, C	protein	325	Bos taurus, Rattus norvegicus	P04695 (AlphaFold model), P10824 (AlphaFold model)
Regulator of G-protein signaling 9	B, D	protein	147	Bos taurus	O46469 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1FQK_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, C)
DARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIVRAMT
TLNIQYGDSARQDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFDRASEYQLN
DSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERK
KWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLN
KKDLFEEKIKKSPLTICYPEYAGSNTYEEAGNYIKVQFLELNMRRDVKEIYSHMTCATDT
QNVKFVFDAVTDIIIKENLKDCGLF

Sequence of entity 2 (B, D), FASTA

>1FQK_2 Regulator of G-protein signaling 9 (chains B, D)
QFWDLNAKLVDIPTKMRVERWAFNFSELIRDPKGRQSFQHFLRKEFSGENLGFWEACEDL
KYGDQSKVKEKAEEIYKLFLAPGARRWINIDGKTMDITVKGLKHPHRYVLDAAQTHIYML
MKKDSYARYLKSPIYKEMLAKAIEPQG

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2
ALF	Tetrafluoroaluminate ion	Al F4	2
MG	Magnesium ion	Mg	2

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:

1TAD 1.7 Å, Gtpase mechanism of gproteins from the 1.7-Å crystal structure of transducin…
1TAG 1.8 Å, Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein
1GOT 2.0 Å, Heterotrimeric complex of a gt-alpha/gi-alpha chimera and the gt-beta-gamma subunits
1FQJ 2.02 Å, Crystal structure of the heterotrimeric complex of the rgs domain of RGS9, the gamma…
1TND 2.2 Å, The 2.2 Å crystal structure of transducin-alpha complexed with GTP gamma S
4J4Q 2.65 Å, Crystal structure of active conformation of GPCR opsin stabilized by octylglucoside
3PQR 2.85 Å, Crystal structure of Metarhodopsin II in complex with a C-terminal peptide derived from…
3V00 2.9 Å, Studies of a constitutively active G-alpha subunit provide insights into the mechanism…
4BEY 2.9 Å, Night blindness causing G90D rhodopsin in complex with GaCT2 peptide
2X72 3.0 Å, Crystal structure of the constitutively active E113Q,D2C,D282C rhodopsin mutant with…
3DQB 3.2 Å, Crystal structure of the active G-protein-coupled receptor opsin in complex with a…
7JSN 3.2 Å, Structure of the Visual Signaling Complex between Transducin and Phosphodiesterase 6

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