1GDD: Gi alpha 1

Tertiary and quaternary structural changes in GIA1 induced by GTP hydrolysis. Determined by X-ray diffraction at 2.2 Å resolution. Released 27 Nov 1995.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: Rattus norvegicus
Chains: 1
Atoms: 2,699
Mol. weight: 40.81 kDa
Ligands: GDP
Released: 27 Nov 1995

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

Secondary structure: helices and β-sheets

1GDD contains 23 α-helices and 7 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: 23 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	10-16	7
α-helix	20-23	4
α-helix	27-29	3
α-helix	31	1
β-strand	32-40	9	1
α-helix	46-57	12
α-helix	63-67	5
α-helix	70-91	22
α-helix	100-112	13
α-helix	121-132	12
α-helix	134-141	8
α-helix	143-145	3
α-helix	152-157	6
α-helix	159-163	5
α-helix	171-176	6
β-strand	185-191	7	1
β-strand	194-200	7	1
β-strand	220-226	7	1
α-helix	227-230	4
α-helix	242-255	14
α-helix	257-261	5
β-strand	263-269	7	1
α-helix	271-280	10
α-helix	283-285	3
α-helix	296-308	13
β-strand	319-323	5	1
α-helix	329-347	19
α-helix	348-350	3
α-helix	351-352	2
β-strand	353	1	1

Molecules and chains

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

Sequence of entity 1 (A), FASTA

>1GDD_1 GI ALPHA 1 (chains A)
GCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGY
SEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDAARADDARQLFVLAGAAEEGFMTA
ELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKT
TGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMN
RMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAA
YIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF

Ligands and cofactors

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

Water and common crystallization additives (SO4) are not listed.

Primary citation

Tertiary and quaternary structural changes in Gi alpha 1 induced by GTP hydrolysis. Mixon, M.B., Lee, E., Coleman, D.E. et al. Science (1995) 270:954-960. 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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