3UMS: G202A mutant of human G-alpha-i1

Crystal structure of the G202A mutant of human G-alpha-i1. Determined by X-ray diffraction at 2.34 Å resolution. Released 8 Feb 2012.

Method: X-ray diffraction
Resolution: 2.34 Å
Organism: Homo sapiens
Chains: 1
Atoms: 2,858
Mol. weight: 41 kDa
Ligands: GDP
Released: 8 Feb 2012

Explore 3UMS in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3UMS contains 24 α-helices and 9 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: 24 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	7-16	10
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	100-113	14
α-helix	121-132	12
α-helix	134-140	7
α-helix	143-145	3
α-helix	152-157	6
α-helix	159-163	5
α-helix	171-175	5
β-strand	184-191	8	1
β-strand	194-201	8	1
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	296-308	13
α-helix	314-316	3
β-strand	319-323	5	1
α-helix	329-346	18
α-helix	348-350	3
α-helix	351-352	2
β-strand	353	1	1

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanine nucleotide-binding protein G(i) subunit alpha-1	A	protein	354	Homo sapiens	P63096 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3UMS_1 Guanine nucleotide-binding protein G(i) subunit alpha-1 (chains A)
MGCTLSAEDKAAVERSKMIDRNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAG
YSEEECKQYKAVVYSNTIQSIIAIIRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMT
AELAGVIKRLWKDSGVQACFNRSREYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVK
TTGIVETHFTFKDLHFKMFDVAGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEM
NRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAA
AYIQCQFEDLNKRKDTKEIYTHFTCATDTKNVQFVFDAVTDVIIKNNLKDCGLF

Ligands and cofactors

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

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

Primary citation

Correction for Regulators of G-protein Signaling accelerate GPCR signaling kinetics and govern sensitivity solely by accelerating GTPase activity. Lambert, N.A., Johnston, C.A., Cappell, S.D. et al. Proc Natl Acad Sci U S A (2012). DOI 10.1073/pnas.1200427109

Other PDB entries of the same protein (UniProt P63096 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6CRK 2.0 Å, Heterotrimeric G-protein in complex with an antibody fragment
3UMR 2.04 Å, Crystal structure of the G202D mutant of human G-alpha-i1
9P7Z 2.1 Å, NTSR1-Gi-NTS(8-13) Complex in the Canonical, AHD Open State (C-Open-Apo)
2OM2 2.2 Å, Crystal Structure Of Human G[alpha]i1 Bound To The Goloco Motif Of Rgs14
8YN9 2.3 Å, Cryo-EM structure of histamine H4 receptor in complex with histamine and Gi
9HYI 2.3 Å, DP81-bound serotonin 5-HT1A receptor - Gi Protein Complex
9O36 2.3 Å, CryoEM structure of mu-opioid receptor - Gi protein complex bound to fluornitrazene (FNZ)
9P80 2.3 Å, NTSR1-Gi-NTS(8-13) Complex in the Non-Canonical, AHD Open State (NC-Open-Apo)
8XXV 2.33 Å, Cryo-EM Structure of the Prostaglandin D2 Receptor 2-indomethacin Coupled to G Protein
3ONW 2.38 Å, Structure of a G-alpha-i1 mutant with enhanced affinity for the RGS14 GoLoco motif.
20ZG 2.4 Å, Cryo-EM structure of the human neurotensin receptor 1 (hNTSR1)-Gi1 complex in the…
20ZH 2.4 Å, Cryo-EM structure of the human neurotensin receptor 1 (hNTSR1)-Gi1 complex in the…

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