3SEA: Rheb-Y35A mutant in GDP- and GMPPNP-bound forms

Structure of Rheb-Y35A mutant in GDP- and GMPPNP-bound forms. Determined by X-ray diffraction at 2.0 Å resolution. Released 20 Jun 2012.

Method
X-ray diffraction
Resolution
2.0 Å
Organism
Homo sapiens
Chains
2
Atoms
3,091
Mol. weight
38.59 kDa
Ligands
GNP, GDP, MG
Released
20 Jun 2012

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

Secondary structure: helices and β-sheets

3SEA contains 13 α-helices and 12 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: 5 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand5-1391
α-helix19-2810
β-strand41-4991
β-strand52-6091
β-strand80-8671
α-helix90-10718
β-strand114-11961
α-helix124-1263
α-helix131-14010
β-strand144-14741
α-helix153-16715
Chain B: 8 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand5-1392
α-helix19-2810
α-helix35-384
β-strand40-49102
β-strand52-61102
α-helix62-632
α-helix72-754
β-strand80-8672
α-helix90-10718
β-strand114-11962
α-helix124-1263
α-helix131-14010
β-strand144-14742
α-helix153-16715

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
GTP-binding protein RhebA, Bprotein167Homo sapiensQ15382 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>3SEA_1 GTP-binding protein Rheb (chains A, B)
QSKSRKIAILGYRSVGKSSLTIQFVEGQFVDSADPTIENTFTKLITVNGQEYHLQLVDTA
GQDEYSIFPQTYSIDINGYILVYSVTSIKSFEVIKVIHGKLLDMVGKVQIPIMLVGNKKD
LHMERVISYEEGKALAESWNAAFLESSAKENQTAVDVFRRIILEAEK

Ligands and cofactors

IDNameFormulaCopies
GNPPhosphoaminophosphonic acid-guanylate esterC10 H17 N6 O13 P31
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P21
MGMagnesium ionMg2

Water and common crystallization additives (ACT) are not listed.

Primary citation

An Autoinhibited Noncanonical Mechanism of GTP Hydrolysis by Rheb Maintains mTORC1 Homeostasis. Mazhab-Jafari, M.T., Marshall, C.B., Ishiyama, N. et al. Structure (2012) 20:1528-1539. DOI 10.1016/j.str.2012.06.013 · PubMed

Other PDB entries of the same protein (UniProt Q15382 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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