1GOT: Gt-alpha/gi-alpha chimera

Heterotrimeric complex of a gt-alpha/gi-alpha chimera and the gt-beta-gamma subunits. Determined by X-ray diffraction at 2.0 Å resolution. Released 12 Mar 1997.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Bos taurus
Chains: 3
Atoms: 6,448
Mol. weight: 87.14 kDa
Ligands: GDP
Released: 12 Mar 1997

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

Secondary structure: helices and β-sheets

1GOT contains 31 α-helices and 37 β-strands across 3 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: 21 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	7-27	21
β-strand	29-36	8	1
α-helix	42-53	12
α-helix	59-64	6
α-helix	66-86	21
α-helix	95-107	13
α-helix	111	1
α-helix	117-128	12
α-helix	130-137	8
α-helix	139-141	3
α-helix	148-152	5
α-helix	155-159	5
α-helix	167-171	5
β-strand	179-187	9	1
β-strand	190-199	10	1
α-helix	204-206	3
α-helix	208-211	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	316-319	4	1
α-helix	325-340	16

Chain B: 4 helices, 29 β-strands

Element	Residues	Length	Sheet
α-helix	3-24	22
α-helix	30-33	4
α-helix	38-39	2
β-strand	47-51	5	3
β-strand	58-63	6	4
β-strand	69-74	6	4
β-strand	78-83	6	4
β-strand	89-94	6	4
α-helix	95	1
β-strand	100-105	6	5
β-strand	111-116	6	5
β-strand	120-125	6	5
β-strand	131	1	4
β-strand	134-140	7	5
β-strand	146-153	8	6
β-strand	156-161	6	6
β-strand	166-170	5	6
β-strand	175-180	6	6
β-strand	187-192	6	7
β-strand	198-203	6	7
β-strand	208-212	5	7
β-strand	218-222	5	7
β-strand	229-234	6	8
β-strand	240-245	6	8
β-strand	250-254	5	8
β-strand	259-264	6	8
β-strand	273-278	6	9
β-strand	284-289	6	9
β-strand	293-298	6	9
β-strand	304-309	6	9
β-strand	315-320	6	3
β-strand	327-331	5	3
β-strand	336-339	4	3

Chain G: 6 helices, 0 β-strands

Element	Residues	Length
α-helix	11-25	15
α-helix	30-32	3
α-helix	33-47	15
α-helix	48-50	3
α-helix	52-55	4
α-helix	59-61	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Gt-alpha/gi-alpha chimera	A	protein	350	Bos taurus	P04695 (AlphaFold model)
Gt-beta	B	protein	340	Bos taurus	P62871 (AlphaFold model)
Gt-gamma	G	protein	73	Bos taurus	P02698 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1GOT_1 GT-ALPHA/GI-ALPHA CHIMERA (chains A)
MGAGASAEEKHSRELEKKLKEDAEKDARTVKLLLLGAGESGKSTIVKQMKIIHQDGYSLE
ECLEFIAIIYGNTLQSILAIVRAMTTLNIQYGDSARQDDARKLMHMADTIEEGTMPKEMS
DIIQRLWKDSGIQACFDRASEYQLNDSAGYYLSDLERLVTPGYVPTEQDVLRSRVKTTGI
IETQFSFKDLNFRMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMH
ESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAGNYIK
VQFLELNMRRDVKEIYSHMTCATDTQNVKFVFDAVTDIIIKENLKDCGLF

Sequence of entity 2 (B), FASTA

>1GOT_2 GT-BETA (chains B)
MSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYA
MHWGTDSRLLLSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNI
CSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTF
TGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNA
FATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDAL
KADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN

Sequence of entity 3 (G), FASTA

>1GOT_3 GT-GAMMA (chains G)
MPVINIEDPVINIEDLTEKDKLKMEVDQLKKEVTLERMLVSKCCEEFRDYVEERSGEDPL
VKGIPEDKNPFKE

Ligands and cofactors

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

Primary citation

The 2.0 A crystal structure of a heterotrimeric G protein. Lambright, D.G., Sondek, J., Bohm, A. et al. Nature (1996) 379:311-319. DOI 10.1038/379311a0 · 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
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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