4G5O: LGN GL4/Galphai3(Q147L) complex

Structure of LGN GL4/Galphai3(Q147L) 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
11,190
Mol. weight
168.59 kDa
Ligands
GDP, CIT
Released
5 Sept 2012

Explore 4G5O in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4G5O contains 82 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: 18 helices, 7 β-strands

ElementResiduesLengthSheet
β-strand33-3971
α-helix46-5712
α-helix63-686
α-helix70-9122
α-helix100-11011
α-helix121-13212
α-helix134-1418
α-helix143-1453
α-helix152-1565
α-helix159-1624
α-helix171-1755
β-strand17912
β-strand185-19171
β-strand194-20071
α-helix210-2134
β-strand220-22671
α-helix227-2315
α-helix242-25413
α-helix257-2593
β-strand263-26971
α-helix271-28010
α-helix283-2853
α-helix296-30813
β-strand319-32351
α-helix329-34719
Chain B: 18 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand33-3973
α-helix46-5712
α-helix63-9129
α-helix100-11011
α-helix113-1164
α-helix121-13212
α-helix134-1418
α-helix143-1453
α-helix152-1576
α-helix159-1624
α-helix171-1766
β-strand17914
β-strand185-19173
β-strand194-20073
α-helix209-2135
β-strand220-22673
α-helix227-2293
α-helix242-25413
α-helix257-2593
β-strand263-26973
α-helix271-28010
α-helix283-2853
α-helix296-30813
β-strand319-32353
α-helix329-34517
Chain C: 20 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand32-3985
α-helix46-5712
α-helix63-686
α-helix70-9021
α-helix98-1003
α-helix101-11010
α-helix121-13212
α-helix134-1407
α-helix143-1453
α-helix152-1576
α-helix159-1624
α-helix171-1755
β-strand17916
β-strand185-19175
β-strand194-20075
α-helix208-2136
β-strand220-22675
α-helix227-2315
α-helix232-2343
α-helix242-25413
α-helix257-2593
β-strand263-26975
α-helix271-2777
α-helix283-2853
α-helix296-30813
β-strand319-32355
α-helix329-34921
Chain D: 18 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand32-3987
α-helix46-5712
α-helix63-9129
α-helix100-11011
α-helix111-1133
α-helix121-13212
α-helix134-1407
α-helix143-1453
α-helix152-1565
α-helix159-1624
α-helix171-1766
β-strand17918
β-strand185-19177
β-strand194-20077
α-helix208-2136
β-strand220-22677
α-helix227-2315
α-helix242-25413
α-helix257-2593
β-strand263-26977
α-helix271-2777
α-helix283-2853
α-helix296-30813
β-strand319-32357
α-helix329-35022
Chains E and F: 2 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix624-63310
α-helix637-6393
β-strand64112
Chain G: 2 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix624-6318
α-helix637-6393
β-strand64116
Chain H: 2 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix625-6339
α-helix637-6393
β-strand64118

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Guanine nucleotide-binding protein G(k) subunit alphaA, B, C, Dprotein330Homo sapiensP08754 (AlphaFold model)
G-protein-signaling modulator 2E, F, G, Hprotein26Mus musculusQ8VDU0 (AlphaFold model)
Sequence of entity 1 (A, B, C, D), FASTA
>4G5O_1 Guanine nucleotide-binding protein G(k) subunit alpha (chains A, B, C, D)
EDGEKAAKEVKLLLLGAGESGKSTIVKQMKIIHEDGYSEDECKQYKVVVYSNTIQSIIAI
IRAMGRLKIDFGEAARADDARQLFVLAGSAEEGVMTPELAGVIKRLWRDGGVQACFSRSR
EYLLNDSASYYLNDLDRISQSNYIPTQQDVLRTRVKTTGIVETHFTFKDLYFKMFDVGGQ
RSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTETSI
ILFLNKKDLFEEKIKRSPLTICYPEYTGSNTYEEAAAYIQCQFEDLNRRKDTKEIYTHFT
CATDTKNVQFVFDAVTDVIIKNNLKECGLY
Sequence of entity 2 (E, F, G, H), FASTA
>4G5O_2 G-protein-signaling modulator 2 (chains E, F, G, H)
DEDFFSLILRSQAKRMDEQRVLLQRD

Ligands and cofactors

IDNameFormulaCopies
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P24
CITCitric acidC6 H8 O74

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:

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