3SF4: G-protein-signaling modulator 2

Crystal structure of the complex between the conserved cell polarity proteins Inscuteable and LGN. Determined by X-ray diffraction at 2.6 Å resolution. Released 23 Nov 2011.

Method
X-ray diffraction
Resolution
2.6 Å
Organism
Homo sapiens
Chains
6
Atoms
9,330
Mol. weight
151.64 kDa
Released
23 Nov 2011

Explore 3SF4 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3SF4 contains 57 α-helices and 8 β-strands across 6 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, 1 β-strand

ElementResiduesLengthSheet
α-helix14-163
α-helix17-2913
α-helix33-4614
α-helix51-6717
α-helix71-8717
α-helix91-10717
α-helix111-12818
α-helix131-15020
α-helix165-18723
α-helix191-20818
β-strand21011
α-helix211-22717
α-helix231-24717
α-helix251-26717
α-helix271-28717
α-helix291-30717
α-helix311-32818
α-helix331-34717
α-helix351-36919
Chain B: 17 helices, 1 β-strand
ElementResiduesLengthSheet
α-helix22-287
α-helix33-4614
α-helix51-6717
α-helix71-8717
α-helix91-10818
α-helix111-12717
α-helix131-15121
α-helix165-18723
α-helix191-20818
β-strand21011
α-helix211-22717
α-helix231-24616
α-helix251-26717
α-helix271-28717
α-helix291-30717
α-helix311-32818
α-helix331-34717
α-helix351-36919
Chain C: 17 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix17-3014
α-helix33-4614
α-helix51-6717
α-helix71-8717
α-helix91-10717
α-helix111-12717
α-helix131-15121
α-helix165-18824
α-helix191-20818
α-helix211-22818
α-helix231-24818
α-helix251-26818
α-helix271-28717
α-helix291-30717
α-helix311-32818
α-helix331-34717
α-helix351-36616
Chains D and F: 2 helices, 2 β-strands
ElementResiduesLengthSheet
α-helix26-3510
β-strand45-4842
α-helix56-583
β-strand62-6542
Chain E: 1 helix, 2 β-strands
ElementResiduesLengthSheet
α-helix26-3510
β-strand45-4733
β-strand63-6533

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
G-protein-signaling modulator 2A, B, Cprotein406Homo sapiensP81274 (AlphaFold model)
Protein inscuteable homologD, E, Fprotein52Homo sapiensQ1MX18 (AlphaFold model)
Sequence of entity 1 (A, B, C), FASTA
>3SF4_1 G-protein-signaling modulator 2 (chains A, B, C)
GPGSMEASCLELALEGERLCKSGDCRAGVSFFEAAVQVGTEDLKTLSAIYSQLGNAYFYL
HDYAKALEYHHHDLTLARTIGDQLGEAKASGNLGNTLKVLGNFDEAIVCCQRHLDISREL
NDKVGEARALYNLGNVYHAKGKSFGCPGPQDVGEFPEEVRDALQAAVDFYEENLSLVTAL
GDRAAQGRAFGNLGNTHYLLGNFRDAVIAHEQRLLIAKEFGDKAAERRAYSNLGNAYIFL
GEFETASEYYKKTLLLARQLKDRAVEAQSCYSLGNTYTLLQDYEKAIDYHLKHLAIAQEL
NDRIGEGRACWSLGNAYTALGNHDQAMHFAEKHLEISREVGDKSGELTARLNLSDLQMVL
GLSYSTNNSIMSENTEIDSSLNGVRPKLGRRHSMENMELMKLTPEK
Sequence of entity 2 (D, E, F), FASTA
>3SF4_2 Protein inscuteable homolog (chains D, E, F)
GPLGSMQVDSVQRWMEDLKLMTECECMCVLQAKPISLEEDAQGDLILAGGPG

Primary citation

Structural basis for interaction between the conserved cell polarity proteins Inscuteable and Leu-Gly-Asn repeat-enriched protein (LGN). Yuzawa, S., Kamakura, S., Iwakiri, Y. et al. Proc Natl Acad Sci U S A (2011) 108:19210-19215. DOI 10.1073/pnas.1110951108 · PubMed

Other PDB entries of the same protein (UniProt P81274 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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