4G5Q: LGN GL4/Galphai1 complex

Structure of LGN GL4/Galphai1 complex. Determined by X-ray diffraction at 2.9 Å resolution. Released 5 Sept 2012.

Method: X-ray diffraction
Resolution: 2.9 Å
Organisms: Homo sapiens, Mus musculus
Chains: 8
Atoms: 11,211
Mol. weight: 167.5 kDa
Ligands: CIT, GDP
Released: 5 Sept 2012

Explore 4G5Q in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4G5Q contains 79 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: 17 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	100-110	11
α-helix	121-132	12
α-helix	134-141	8
α-helix	142-145	4
α-helix	152-157	6
α-helix	159-162	4
α-helix	171-176	6
β-strand	179	1	2
β-strand	185-190	6	1
β-strand	195-200	6	1
α-helix	208-214	7
β-strand	220-226	7	1
α-helix	227-231	5
α-helix	242-254	13
β-strand	263-269	7	1
α-helix	271-278	8
α-helix	283-285	3
α-helix	296-308	13
β-strand	319-323	5	1
α-helix	329-346	18

Chain B: 19 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	100-110	11
α-helix	113-116	4
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	179	1	4
β-strand	185-190	6	3
β-strand	195-200	6	3
α-helix	209-213	5
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	329-348	20

Chain C: 16 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	32-39	8	5
α-helix	46-57	12
α-helix	63-90	28
α-helix	100-110	11
α-helix	121-132	12
α-helix	134-140	7
α-helix	143-145	3
α-helix	152-157	6
α-helix	159-162	4
α-helix	171-175	5
β-strand	179	1	6
β-strand	185-191	7	5
β-strand	194-200	7	5
α-helix	208-213	6
β-strand	220-226	7	5
α-helix	227-231	5
α-helix	242-254	13
β-strand	263-269	7	5
α-helix	271-277	7
α-helix	283-285	3
α-helix	296-308	13
β-strand	319-323	5	5
α-helix	329-350	22

Chain D: 19 helices, 7 β-strands

Element	Residues	Length	Sheet
β-strand	32-39	8	7
α-helix	46-57	12
α-helix	63-68	6
α-helix	70-90	21
α-helix	93-95	3
α-helix	100-109	10
α-helix	110-112	3
α-helix	121-132	12
α-helix	134-140	7
α-helix	143-145	3
α-helix	152-157	6
α-helix	159-162	4
α-helix	171-176	6
β-strand	179	1	8
β-strand	185-191	7	7
β-strand	194-200	7	7
α-helix	208-213	6
β-strand	220-226	7	7
α-helix	227-231	5
α-helix	242-254	13
β-strand	263-269	7	7
α-helix	271-277	7
α-helix	283-285	3
α-helix	296-308	13
β-strand	319-323	5	7
α-helix	329-350	22

Chains E, F and G: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	624-633	10
α-helix	637-639	3
β-strand	641	1	2

Chain H: 2 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	625-633	9
α-helix	637-639	3
β-strand	641	1	8

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanine nucleotide-binding protein G(i) subunit alpha-1	A, B, C, D	protein	330	Homo sapiens	P63096 (AlphaFold model)
G-protein-signaling modulator 2	E, F, G, H	protein	25	Mus musculus	Q8VDU0 (AlphaFold model)

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

>4G5Q_1 Guanine nucleotide-binding protein G(i) subunit alpha-1 (chains A, B, C, D)
EDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEAGYSEEECKQYKAVVYSNTIQSIIAI
IRAMGRLKIDFGDSARADDARQLFVLAGAAEEGFMTAELAGVIKRLWKDSGVQACFNRSR
EYQLNDSAAYYLNDLDRIAQPNYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQ
RSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSI
ILFLNKKDLFEEKIKKSPLTICYPEYAGSNTYEEAAAYIQCQFEDLNKRKDTKEIYTHFT
CATDTKNVQFVFDAVTDVIIKNNLKDCGLF

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

>4G5Q_2 G-protein-signaling modulator 2 (chains E, F, G, H)
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 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
3UMS 2.34 Å, Crystal structure of the G202A mutant of human G-alpha-i1
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…

Browse structure collections

About this viewer

MolViewer shows 4G5Q directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.