4G2V: Structure complex of LGN binding with FRMPD1

Structure complex of LGN binding with FRMPD1. Determined by X-ray diffraction at 2.4 Å resolution. Released 23 Jan 2013.

Method: X-ray diffraction
Resolution: 2.4 Å
Organisms: Mus musculus, Homo sapiens
Chains: 2
Atoms: 2,732
Mol. weight: 42.67 kDa
Ligands: BTB
Released: 23 Jan 2013

Explore 4G2V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4G2V contains 17 α-helices and 0 β-strands across 2 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: 16 helices, 0 β-strands

Element	Residues	Length
α-helix	14-29	16
α-helix	33-46	14
α-helix	51-67	17
α-helix	71-87	17
α-helix	91-108	18
α-helix	111-127	17
α-helix	131-151	21
α-helix	165-188	24
α-helix	191-208	18
α-helix	211-228	18
α-helix	231-247	17
α-helix	251-267	17
α-helix	271-287	17
α-helix	291-307	17
α-helix	311-327	17
α-helix	332-343	12

Chain B: 1 helix, 0 β-strands

Element	Residues	Length	Sheet
α-helix	7-10	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
G-protein-signaling modulator 2	A	protein	340	Mus musculus	Q8VDU0 (AlphaFold model)
peptide from FERM and PDZ domain-containing protein 1	B	protein	38	Homo sapiens	Q5SYB0 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>4G2V_1 G-protein-signaling modulator 2 (chains A)
GPGSASCLELALEGERLCKSGDCRAGVSFFEAAVQVGTEDLKTLSAIYSQLGNAYFYLHD
YAKALEYHHHDLTLARTIGDQLGEAKASGNLGNTLKVLGNFDEAIVCCQRHLDISRELND
KVGEARALYNLGNVYHAKGKSFGCPGPQDTGEFPEDVRNALQAAVDLYEENLSLVTALGD
RAAQGRAFGNLGNTHYLLGNFRDAVIAHEQRLLIAKEFGDKAAERRAYSNLGNAYIFLGE
FETASEYYKKTLLLARQLKDRAVEAQSCYSLGNTYTLLQDYEKAIDYHLKHLAIAQELKD
RIGEGRACWSLGNAYTALGNHDQAMHFAEKHLEISREVGD

Sequence of entity 2 (B), FASTA

>4G2V_2 peptide from FERM and PDZ domain-containing protein 1 (chains B)
ALGLLAPLRETKSTNPASRVMEMEPETMETKSVIDSRV

Ligands and cofactors

ID	Name	Formula	Copies
BTB	2-[bis-(2-hydroxy-ethyl)-amino]-2-hydroxymethyl-propane-1,3-diol	C8 H19 N O5	1

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

Primary citation

Structural and biochemical characterization of the interaction between LGN and Frmpd1. Pan, Z., Shang, Y., Jia, M. et al. J Mol Biol (2013) 425:1039-1049. DOI 10.1016/j.jmb.2013.01.003 · PubMed

Other PDB entries of the same protein (UniProt Q8VDU0 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3RO3 1.1 Å, crystal structure of LGN/mInscuteable complex
3RO2 2.3 Å, Structures of the LGN/NuMA complex
7EP7 2.6 Å, The complex structure of Gpsm2 and Whirlin
4JHR 2.8 Å, An auto-inhibited conformation of LGN reveals a distinct interaction mode between GoLoco…
4G5O 2.9 Å, Structure of LGN GL4/Galphai3(Q147L) complex
4G5Q 2.9 Å, Structure of LGN GL4/Galphai1 complex
4G5R 3.48 Å, Structure of LGN GL4/Galphai3 complex
4G5S 3.62 Å, Structure of LGN GL3/Galphai3 complex

Browse structure collections

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