1TAG: Transducin-alpha

Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein. Determined by X-ray diffraction at 1.8 Å resolution. Released 7 Feb 1995.

Method: X-ray diffraction
Resolution: 1.8 Å
Organism: Bos taurus
Chains: 1
Atoms: 2,890
Mol. weight: 37.61 kDa
Ligands: GDP, MG
Released: 7 Feb 1995

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

Secondary structure: helices and β-sheets

1TAG contains 18 α-helices and 8 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: 18 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	28-35	8	1
α-helix	42-53	12
α-helix	59-86	28
α-helix	96-109	14
α-helix	111	1
α-helix	117-128	12
α-helix	130-136	7
α-helix	139-142	4
α-helix	148-152	5
α-helix	155-158	4
α-helix	167-172	6
β-strand	182-187	6	1
β-strand	190-197	8	1
α-helix	201-208	8
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	316-319	4	1
α-helix	325-339	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transducin-alpha	A	protein	324	Bos taurus	P04695 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1TAG_1 TRANSDUCIN-ALPHA (chains A)
ARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLEECLEFIAIIYGNTLQSILAIVRAMTT
LNIQYGDSARQDDARKLMHMADTIEEGTMPKEMSDIIQRLWKDSGIQACFDRASEYQLND
SAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGIIETQFSFKDLNFRMFDVGGQRSERKK
WIHCFEGVTCIIFIAALSAYDMVLVEDDEVNRMHESLHLFNSICNHRYFATTSIVLFLNK
KDVFSEKIKKAHLSICFPDYNGPNTYEDAGNYIKVQFLELNMRRDVKEIYSHMTCATDTQ
NVKFVFDAVTDIIIKENLKDCGLF

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1
MG	Magnesium ion	Mg	1

Primary citation

Structural determinants for activation of the alpha-subunit of a heterotrimeric G protein. Lambright, D.G., Noel, J.P., Hamm, H.E. et al. Nature (1994) 369:621-628. DOI 10.1038/369621a0 · 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…
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
1FQK 2.3 Å, Crystal structure of the heterodimeric complex of the rgs domain of RGS9, and the GT/I1…
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

Browse structure collections

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