1GP2: G protein gi alpha 1

G protein heterotrimer GI_ALPHA_1 BETA_1 GAMMA_2 with GDP bound. Determined by X-ray diffraction at 2.3 Å resolution. Released 12 Feb 1997.

Method: X-ray diffraction
Resolution: 2.3 Å
Organisms: Rattus norvegicus, Bos taurus
Chains: 3
Atoms: 6,197
Mol. weight: 85.97 kDa
Ligands: GDP
Released: 12 Feb 1997

Explore 1GP2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1GP2 contains 26 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: 20 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	10-29	20
β-strand	33-39	7	1
α-helix	46-56	11
α-helix	63-67	5
α-helix	70-91	22
α-helix	100-110	11
α-helix	121-132	12
α-helix	134-141	8
α-helix	152-157	6
α-helix	159-163	5
α-helix	171-176	6
α-helix	184	1
β-strand	185-191	7	1
β-strand	194-200	7	1
α-helix	208-211	4
α-helix	212-215	4
β-strand	220-226	7	1
α-helix	227-231	5
β-strand	233	1	2
β-strand	241	1	2
α-helix	242-254	13
α-helix	257-259	3
β-strand	263-269	7	1
α-helix	271-280	10
α-helix	283-285	3
α-helix	296-309	14
β-strand	319	1	1
β-strand	322-323	2	1
α-helix	329-346	18

Chain B: 4 helices, 28 β-strands

Element	Residues	Length	Sheet
α-helix	4-25	22
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
β-strand	100-105	6	5
β-strand	111-116	6	5
β-strand	120-125	6	5
β-strand	137-140	4	5
β-strand	146-153	8	6
β-strand	156-161	6	6
β-strand	166-170	5	6
α-helix	171-173	3
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	217-222	6	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
α-helix	272	1
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: 2 helices, 0 β-strands

Element	Residues	Length	Sheet
α-helix	9-23	15
α-helix	30-44	15

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
G protein gi alpha 1	A	protein	353	Rattus norvegicus	P10824 (AlphaFold model)
G protein gi beta 1	B	protein	340	Bos taurus	P62871 (AlphaFold model)
G protein gi gamma 2	G	protein	71	Bos taurus	P63212 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1GP2_1 G PROTEIN GI ALPHA 1 (chains A)
GCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGY
SEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTA
ELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKT
TGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMN
RMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAA
YIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF

Sequence of entity 2 (B), FASTA

>1GP2_2 G PROTEIN GI BETA 1 (chains B)
MSELDQLRQEAEQLKNQIRDARKACADATLSQITNNIDPVGRIQMRTRRTLRGHLAKIYA
MHWGTDSRLLVSASQDGKLIIWDSYTTNKVHAIPLRSSWVMTCAYAPSGNYVACGGLDNI
CSIYNLKTREGNVRVSRELAGHTGYLSCCRFLDDNQIVTSSGDTTCALWDIETGQQTTTF
TGHTGDVMSLSLAPDTRLFVSGACDASAKLWDVREGMCRQTFTGHESDINAICFFPNGNA
FATGSDDATCRLFDLRADQELMTYSHDNIICGITSVSFSKSGRLLLAGYDDFNCNVWDAL
KADRAGVLAGHDNRVSCLGVTDDGMAVATGSWDSFLKIWN

Sequence of entity 3 (G), FASTA

>1GP2_3 G PROTEIN GI GAMMA 2 (chains G)
MASNNTASIAQARKLVEQLKMEANIDRIKVSKAAADLMAYCEAHAKEDPLLTPVPASENP
FREKKFFSAIL

Ligands and cofactors

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

Primary citation

The structure of the G protein heterotrimer Gi alpha 1 beta 1 gamma 2. Wall, M.A., Coleman, D.E., Lee, E. et al. Cell (1995) 83:1047-1058. DOI 10.1016/0092-8674(95)90220-1 · PubMed

Other PDB entries of the same protein (UniProt P10824 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1CIP 1.5 Å, Gi-alpha-1 subunit of guanine nucleotide-binding protein complexed with a GTP analogue
1SVS 1.5 Å, Structure of the K180P mutant of Gi alpha subunit bound to GppNHp.
4N0D 1.55 Å, Crystal structure of the K345L variant of the Gi alpha1 subunit bound to GTPgammaS
5KDO 1.9 Å, Heterotrimeric complex of the 4 alanine insertion variant of the Gi alpha1 subunit and…
1AS0 2.0 Å, GTP-gamma-S bound G42V GIA1
1GIA 2.0 Å, Structure of active conformations of GIA1 and the mechanism of GTP hydrolysis
1SVK 2.0 Å, Structure of the K180P mutant of Gi alpha subunit bound to AlF4 and GDP
4PAQ 2.0 Å, A conserved phenylalanine as relay between the 5 helix and the GDP binding region of…
4PAO 2.0 Å, A conserved phenylalanine as relay between the 5 helix and the GDP binding region of…
1FQJ 2.02 Å, Crystal structure of the heterotrimeric complex of the rgs domain of RGS9, the gamma…
6M8H 2.07 Å, Crystal Structure of the R208Q mutant of G(i) subunit alpha-1
1BH2 2.1 Å, A326S mutant of an inhibitory alpha subunit

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