1GIA: G protein gi alpha 1

Structure of active conformations of GIA1 and the mechanism of GTP hydrolysis. Determined by X-ray diffraction at 2.0 Å resolution. Released 30 Sept 1994.

Method: X-ray diffraction
Resolution: 2.0 Å
Organism: Rattus norvegicus
Chains: 1
Atoms: 2,649
Mol. weight: 40.83 kDa
Ligands: GSP, MG
Released: 30 Sept 1994

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

Secondary structure: helices and β-sheets

1GIA contains 17 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: 17 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	35-39	5	1
α-helix	46-57	12
α-helix	63-90	28
α-helix	100-115	16
α-helix	121-132	12
α-helix	134-140	7
α-helix	143-145	3
α-helix	152-156	5
α-helix	159-162	4
α-helix	171-176	6
β-strand	184-191	8	1
β-strand	194-201	8	1
α-helix	208-214	7
β-strand	220-226	7	1
α-helix	227-231	5
β-strand	233-234	2	2
β-strand	237-241	5	2
α-helix	242-254	13
α-helix	257-259	3
β-strand	263-269	7	1
α-helix	271-277	7
α-helix	283-285	3
α-helix	296-308	13
β-strand	319-323	5	1
α-helix	329-342	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
G protein gi alpha 1	A	protein	353	Rattus norvegicus	P10824 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>1GIA_1 G PROTEIN GI ALPHA 1 (chains A)
GCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGY
SEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTA
ELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKT
TGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMN
RMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAA
YIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF

Ligands and cofactors

ID	Name	Formula	Copies
GSP	5'-guanosine-diphosphate-monothiophosphate	C10 H16 N5 O13 P3 S	1
MG	Magnesium ion	Mg	1

Primary citation

Structures of active conformations of Gi alpha 1 and the mechanism of GTP hydrolysis. Coleman, D.E., Berghuis, A.M., Lee, E. et al. Science (1994) 265:1405-1412. 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
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
4N0E 2.1 Å, Crystal structure of the K345L variant of the Gi alpha1 subunit bound to GDP

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