9B4R: MRAS

Crystal structure of MRAS bound to GMPPNP. Determined by X-ray diffraction at 2.1 Å resolution. Released 22 Jan 2025.

Method
X-ray diffraction
Resolution
2.1 Å
Organism
Homo sapiens
Chains
1
Atoms
1,521
Mol. weight
20.14 kDa
Ligands
ZN, MG, GNP
Released
22 Jan 2025

Explore 9B4R in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

9B4R contains 8 α-helices and 8 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 A: 8 helices, 8 β-strands

ElementResiduesLengthSheet
β-strand13-2081
α-helix26-3510
α-helix491
β-strand50-5671
β-strand59-6791
α-helix75-839
β-strand87-9371
α-helix97-1015
α-helix103-11412
β-strand121-12661
α-helix138-14710
β-strand152-15431
β-strand15612
α-helix1611
β-strand16212
α-helix164-17613

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Ras-related protein M-RasAprotein169Homo sapiensO14807 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>9B4R_1 Ras-related protein M-Ras (chains A)
GLPTYKLVVVGDGGVGKSALTIQFFQKIFVPDYDPTIEDSYLKHTEIDNQWAILDVLDTA
GQEEFSAMREQYMRTGDGFLIVYSVTDKASFEHVDRFHQLILRVKDRESFPMILVANKVD
LMHLRKITREQGKEMATKHNIPYIETSAKDPPLNVDKAFHDLVRVIRQQ

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn2
MGMagnesium ionMg1
GNPPhosphoaminophosphonic acid-guanylate esterC10 H17 N6 O13 P31

Primary citation

Structural insights into isoform-specific RAS-PI3K alpha interactions and the role of RAS in PI3K alpha activation. Czyzyk, D., Yan, W., Messing, S. et al. Nat Commun (2025) 16:525-525. DOI 10.1038/s41467-024-55766-x · PubMed

Other PDB entries of the same protein (UniProt O14807 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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