4G5R: LGN GL4/Galphai3 complex

Structure of LGN GL4/Galphai3 complex. Determined by X-ray diffraction at 3.48 Å resolution. Released 5 Sept 2012.

Method: X-ray diffraction
Resolution: 3.48 Å
Organisms: Homo sapiens, Mus musculus
Chains: 8
Atoms: 10,601
Mol. weight: 166.84 kDa
Ligands: CIT, GDP
Released: 5 Sept 2012

Explore 4G5R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4G5R contains 80 α-helices and 32 β-strands across 8 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: 19 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	33-39	7	1
α-helix	46-57	12
α-helix	63-68	6
α-helix	70-91	22
α-helix	98-100	3
α-helix	101-110	10
α-helix	121-132	12
α-helix	134-140	7
α-helix	152-157	6
α-helix	159-162	4
α-helix	171-175	5
β-strand	179	1	2
β-strand	185-191	7	1
β-strand	194-200	7	1
α-helix	208-213	6
β-strand	220-226	7	1
α-helix	227-231	5
α-helix	232-235	4
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
β-strand	319-323	5	1
α-helix	329-348	20

Chain B: 18 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	33-39	7	3
α-helix	46-57	12
α-helix	63-91	29
α-helix	101-110	10
α-helix	121-132	12
α-helix	134-140	7
α-helix	152-157	6
α-helix	159-162	4
α-helix	171-175	5
β-strand	179	1	4
α-helix	180-181	2
β-strand	185-191	7	3
β-strand	194-200	7	3
α-helix	208-213	6
β-strand	220-226	7	3
α-helix	227-231	5
α-helix	232-235	4
α-helix	242-254	13
α-helix	257-259	3
β-strand	263-269	7	3
α-helix	271-280	10
α-helix	283-285	3
α-helix	296-308	13
β-strand	319-323	5	3
α-helix	329-347	19

Chain C: 19 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	34-39	6	5
α-helix	46-57	12
α-helix	63-68	6
α-helix	70-91	22
α-helix	98-100	3
α-helix	101-110	10
α-helix	111-113	3
α-helix	121-131	11
α-helix	134-140	7
α-helix	152-157	6
α-helix	159-162	4
α-helix	171-175	5
β-strand	179	1	6
β-strand	186-191	6	5
β-strand	194-199	6	5
α-helix	210-213	4
β-strand	220-226	7	5
α-helix	227-231	5
α-helix	242-254	13
α-helix	257-259	3
β-strand	263-269	7	5
α-helix	271-280	10
α-helix	283-285	3
α-helix	296-308	13
β-strand	319-323	5	5
α-helix	329-352	24

Chain D: 20 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	33-39	7	7
α-helix	46-57	12
α-helix	63-68	6
α-helix	70-91	22
α-helix	98-100	3
α-helix	101-110	10
α-helix	121-132	12
α-helix	134-140	7
α-helix	152-157	6
α-helix	159-162	4
α-helix	171-175	5
β-strand	179	1	8
α-helix	180-181	2
β-strand	185-190	6	7
β-strand	195-200	6	7
α-helix	209-213	5
β-strand	220-226	7	7
α-helix	227-231	5
α-helix	232-235	4
α-helix	242-254	13
α-helix	257-259	3
β-strand	263-269	7	7
α-helix	271-280	10
α-helix	283-285	3
α-helix	296-308	13
β-strand	319-323	5	7
α-helix	329-351	23

Chains E, G and Z: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	624-632	9
β-strand	641	1	2

Chain F: 1 helix, 1 β-strand

Element	Residues	Length	Sheet
α-helix	624-633	10
β-strand	641	1	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanine nucleotide-binding protein G(k) subunit alpha	A, B, C, D	protein	330	Homo sapiens	P08754 (AlphaFold model)
G-protein-signaling modulator 2	E, F, G, Z	protein	25	Mus musculus	Q8VDU0 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>4G5R_1 Guanine nucleotide-binding protein G(k) subunit alpha (chains A, B, C, D)
EDGEKAAKEVKLLLLGAGESGKSTIVKQMKIIHEDGYSEDECKQYKVVVYSNTIQSIIAI
IRAMGRLKIDFGEAARADDARQLFVLAGSAEEGVMTPELAGVIKRLWRDGGVQACFSRSR
EYQLNDSASYYLNDLDRISQSNYIPTQQDVLRTRVKTTGIVETHFTFKDLYFKMFDVGGQ
RSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTETSI
ILFLNKKDLFEEKIKRSPLTICYPEYTGSNTYEEAAAYIQCQFEDLNRRKDTKEIYTHFT
CATDTKNVQFVFDAVTDVIIKNNLKECGLY

Sequence of entity 2 (E, F, G, Z), FASTA

>4G5R_2 G-protein-signaling modulator 2 (chains E, F, G, Z)
DEDFFSLILRSQAKRMDEQRVLLQR

Ligands and cofactors

ID	Name	Formula	Copies
CIT	Citric acid	C6 H8 O7	4
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	4

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

Primary citation

Crystal structures of the scaffolding protein LGN reveal the general mechanism by which GoLoco binding motifs inhibit the release of GDP from G alpha i. Jia, M., Li, J., Zhu, J. et al. J Biol Chem (2012) 287:36766-36776. DOI 10.1074/jbc.M112.391607 · PubMed

Other PDB entries of the same protein (UniProt P08754 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2ODE 1.9 Å, Crystal structure of the heterodimeric complex of human RGS8 and activated Gi alpha 3
9YCX 2.1 Å, Neurotensin Receptor 1 (NTSR1) bound to Octotensin in complex with Gi3 in the…
9YCY 2.2 Å, Neurotensin Receptor 1 (NTSR1) bound to Octotensin in complex with Gi3 in the Canonical…
8IKL 2.33 Å, Cryo-EM structure of the CD97-G13 complex
8YK0 2.4 Å, Cryo-EM structure of human GPR156-Gi3 complex
7T10 2.5 Å, CryoEM structure of somatostatin receptor 2 in complex with somatostatin-14 and Gi3
9VJ6 2.62 Å, Cryo-EM structure of 5-HT1AR-Gi3 in complex with F-15599
7T11 2.7 Å, CryoEM structure of somatostatin receptor 2 in complex with Octreotide and Gi3.
9VJF 2.7 Å, Cryo-EM structure of 5-HT1AR-Gi3 in complex with buspirone
2IHB 2.71 Å, Crystal structure of the heterodimeric complex of human RGS10 and activated Gi alpha 3
2V4Z 2.8 Å, The crystal structure of the human G-protein subunit alpha (GNAI3) in complex with an…
7KH0 2.8 Å, Cryo-EM structure of the human arginine vasopressin AVP-vasopressin receptor V2R-Gs…

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