8SDW: Non-myristoylated mutant [L8K]Arf1

Crystal structure of the non-myristoylated mutant [L8K]Arf1 in complex with a GDP analogue. Determined by X-ray diffraction at 1.75 Å resolution. Released 28 Jun 2023.

Method
X-ray diffraction
Resolution
1.75 Å
Organism
Homo sapiens
Chains
1
Atoms
1,651
Mol. weight
21.29 kDa
Ligands
G3D, MG
Released
28 Jun 2023

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

Secondary structure: helices and β-sheets

8SDW contains 9 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: 9 helices, 9 β-strands

ElementResiduesLengthSheet
β-strand18-2471
α-helix30-378
α-helix41-422
β-strand43-4861
β-strand51-5881
β-strand61-6771
α-helix76-838
β-strand87-9371
α-helix97-993
α-helix100-11112
α-helix114-1163
β-strand120-12671
α-helix136-1438
α-helix145-1473
β-strand153-15751
β-strand15912
β-strand16412
α-helix166-17813

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
ADP-ribosylation factor 1Aprotein181Homo sapiensP84077 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>8SDW_1 ADP-ribosylation factor 1 (chains A)
MGNIFANKFKGLFGKKEMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKN
ISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERVNEAREELMRMLAEDELRDAV
LLVFANKQDLPNAMNAAEITDKLGLHSLRHRNWYIQATCATSGDGLYEGLDWLSNQLRNQ
K

Ligands and cofactors

IDNameFormulaCopies
G3DGuanosine-3'-monophosphate-5'-diphosphateC10 H16 N5 O14 P31
MGMagnesium ionMg1

Primary citation

Point mutations in Arf1 reveal cooperative effects of the N-terminal extension and myristate for GTPase-activating protein catalytic activity. Rosenberg Jr., E.M., Jian, X., Soubias, O. et al. PLoS One (2024) 19:e0295103-e0295103. DOI 10.1371/journal.pone.0295103 · PubMed

Other PDB entries of the same protein (UniProt P84077 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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