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
| 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 | 143-145 | 3 | |
| α-helix | 152-156 | 5 | |
| 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 | 210-213 | 4 | |
| β-strand | 220-226 | 7 | 1 |
| α-helix | 227-231 | 5 | |
| 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 | 329-347 | 19 | |
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 | 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 | 159-162 | 4 | |
| α-helix | 171-176 | 6 | |
| β-strand | 179 | 1 | 4 |
| β-strand | 185-191 | 7 | 3 |
| β-strand | 194-200 | 7 | 3 |
| α-helix | 209-213 | 5 | |
| β-strand | 220-226 | 7 | 3 |
| α-helix | 227-229 | 3 | |
| 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 | 329-345 | 17 | |
Chain C: 20 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 32-39 | 8 | 5 |
| α-helix | 46-57 | 12 | |
| α-helix | 63-68 | 6 | |
| α-helix | 70-90 | 21 | |
| α-helix | 98-100 | 3 | |
| α-helix | 101-110 | 10 | |
| 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 | 232-234 | 3 | |
| α-helix | 242-254 | 13 | |
| α-helix | 257-259 | 3 | |
| 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 | 329-349 | 21 | |
Chain D: 18 helices, 7 β-strands
| Element | Residues | Length | Sheet |
|---|
| β-strand | 32-39 | 8 | 7 |
| α-helix | 46-57 | 12 | |
| α-helix | 63-91 | 29 | |
| α-helix | 100-110 | 11 | |
| α-helix | 111-113 | 3 | |
| α-helix | 121-132 | 12 | |
| α-helix | 134-140 | 7 | |
| α-helix | 143-145 | 3 | |
| α-helix | 152-156 | 5 | |
| 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 | |
| α-helix | 257-259 | 3 | |
| 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 and F: 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 G: 2 helices, 1 β-strand
| Element | Residues | Length | Sheet |
|---|
| α-helix | 624-631 | 8 | |
| α-helix | 637-639 | 3 | |
| β-strand | 641 | 1 | 6 |
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(k) subunit alpha | A, B, C, D | protein | 330 | Homo sapiens | P08754 (AlphaFold model) |
| G-protein-signaling modulator 2 | E, F, G, H | protein | 26 | Mus musculus | Q8VDU0 (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
| ID | Name | Formula | Copies |
|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 4 |
| CIT | Citric acid | C6 H8 O7 | 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
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- 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
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Browse structure collections
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