4OH9: Human MST2 SARAH homodimer

Crystal Structure of the human MST2 SARAH homodimer. Determined by X-ray diffraction at 1.7 Å resolution. Released 23 Jul 2014.

Method
X-ray diffraction
Resolution
1.7 Å
Organism
Homo sapiens
Chains
2
Atoms
953
Mol. weight
12.19 kDa
Released
23 Jul 2014

Explore 4OH9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4OH9 contains 4 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.

Chains A and B: 2 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix4-74
α-helix12-5039

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Serine/threonine-protein kinase 3A, Bprotein51Homo sapiensQ13188 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>4OH9_1 Serine/threonine-protein kinase 3 (chains A, B)
GSDFDFLKNLSLEELQMRLKALDPMMEREIEELRQRYTAKRQPILDAMDAK

Primary citation

Structural basis of the heterodimerization of the MST and RASSF SARAH domains in the Hippo signalling pathway. Hwang, E., Cheong, H.K., Mushtaq, A.U. et al. Acta Crystallogr D Biol Crystallogr (2014) 70:1944-1953. DOI 10.1107/S139900471400947X · PubMed

Other PDB entries of the same protein (UniProt Q13188 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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