8FPW: Tumor related RhoA mutant A161V

Crystal structure of tumor related RhoA mutant A161V in complex with GDP. Determined by X-ray diffraction at 1.4 Å resolution. Released 5 Jun 2024.

Method
X-ray diffraction
Resolution
1.4 Å
Organism
Homo sapiens
Chains
1
Atoms
1,756
Mol. weight
21.25 kDa
Ligands
GDP, DIO, MG
Released
5 Jun 2024

Explore 8FPW in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8FPW contains 13 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 A: 13 helices, 6 β-strands

ElementResiduesLengthSheet
α-helix31
β-strand4-1291
α-helix18-236
α-helix29-313
β-strand42-4871
β-strand51-5881
α-helix64-663
α-helix70-734
β-strand79-8571
α-helix89-946
α-helix95-995
α-helix100-1067
β-strand112-11761
α-helix119-1213
α-helix125-1328
α-helix138-1403
α-helix141-15111
β-strand155-15841
α-helix167-18014

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Transforming protein RhoAAprotein183Homo sapiensP61586 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8FPW_1 Transforming protein RhoA (chains A)
GSMAAIRKKLVIVGDGACGKTCLLIVNSKDQFPEVYVPTVFENYVADIEVDGKQVELALW
DTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNK
KDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSVKTKDGVREVFEMATRAA
LQA

Ligands and cofactors

IDNameFormulaCopies
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P21
DIO1,4-diethylene dioxideC4 H8 O22
MGMagnesium ionMg1

Primary citation

Tumor-derived RHOA mutants interact with effectors in the GDP-bound state. Lin, Y., Ramelot, T.A., Senyuz, S. et al. Nat Commun (2024) 15:7176-7176. DOI 10.1038/s41467-024-51445-z · PubMed

Other PDB entries of the same protein (UniProt P61586 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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