1E0S: Small G protein Arf6-GDP

small G protein Arf6-GDP. Determined by X-ray diffraction at 2.28 Å resolution. Released 18 Apr 2000.

Method
X-ray diffraction
Resolution
2.28 Å
Organism
Homo sapiens
Chains
1
Atoms
1,522
Mol. weight
20.52 kDa
Ligands
GDP
Released
18 Apr 2000

Explore 1E0S in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1E0S contains 12 α-helices and 9 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: 12 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix3-97
β-strand14-2181
α-helix26-327
β-strand39-4461
β-strand47-5481
β-strand57-6481
α-helix68-703
α-helix71-744
α-helix75-773
β-strand83-8971
α-helix93-953
α-helix96-10712
α-helix110-1123
β-strand116-12271
α-helix129-1313
α-helix132-1387
α-helix141-1433
β-strand149-15351
β-strand15512
β-strand16012
α-helix162-17211

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ADP-ribosylation factor 6Aprotein174Homo sapiensP62330 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>1E0S_1 ADP-ribosylation factor 6 (chains A)
GKVLSKIFGNKEMRILMLGLDAAGKTTILYKLKLGQSVTTIPTVGFNVETVTYKNVKFNV
WDVGGQDKIRPLWRHYYTGTQGLIFVVDCADRDRIDEARQELHRIINDREMRDAIILIFA
NKQDLPDAMKPHEIQEKLGLTRIRDRNWYVQPSCATSGDGLYEGLTWLTSNYKS

Ligands and cofactors

IDNameFormulaCopies
GDPGuanosine-5'-diphosphateC10 H15 N5 O11 P21

Water and common crystallization additives (NH4, BME) are not listed.

Primary citation

Structure of Arf6-Gdp Suggests a Basis for Guanine Nucleotide Exchange Factors Specificity. Menetrey, J., Macia, E., Pasqualato, S. et al. Nat Struct Biol (2000) 7:466. DOI 10.1038/75863 · PubMed

Other PDB entries of the same protein (UniProt P62330 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

About this viewer

MolViewer shows 1E0S directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.