3I3S: H-Ras with Thr50 replaced by Isoleucine

Crystal Structure of H-Ras with Thr50 replaced by Isoleucine. Determined by X-ray diffraction at 1.36 Å resolution. Released 22 Dec 2009.

Method
X-ray diffraction
Resolution
1.36 Å
Organism
Homo sapiens
Chains
1
Atoms
1,688
Mol. weight
19.52 kDa
Ligands
CA, MG, GNP
Released
22 Dec 2009

Explore 3I3S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3I3S contains 7 α-helices and 6 β-strands across 1 chain. 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 R: 7 helices, 6 β-strands

ElementResiduesLengthSheet
β-strand2-1091
α-helix16-2510
β-strand37-46101
β-strand49-58101
α-helix62-643
α-helix68-714
β-strand77-8371
α-helix87-915
α-helix93-10412
β-strand111-11661
α-helix127-13711
β-strand141-14331
α-helix152-16312

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
GTPase HRasRprotein166Homo sapiensP01112 (AlphaFold model)
Sequence of entity 1 (R), FASTA
>3I3S_1 GTPase HRas (chains R)
MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGEICLLDILDTAG
QEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDL
AARTVESRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQH

Ligands and cofactors

IDNameFormulaCopies
CACalcium ionCa1
MGMagnesium ionMg3
GNPPhosphoaminophosphonic acid-guanylate esterC10 H17 N6 O13 P31

Primary citation

A restricted spectrum of NRAS mutations causes Noonan syndrome. Cirstea, I.C., Kutsche, K., Dvorsky, R. et al. Nat Genet (2010) 42:27-29. DOI 10.1038/ng.497 · PubMed

Other PDB entries of the same protein (UniProt P01112 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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