Crystal structure of human GGA1 GAT domain. Determined by X-ray diffraction at 2.1 Å resolution. Released 20 May 2003.
Explore 1O3X in 3D Show helices and sheets RCSB PDB PDBe
1O3X contains 3 α-helices and 0 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.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 198-234 | 37 | |
| α-helix | 243-267 | 25 | |
| α-helix | 274-299 | 26 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| ADP-ribosylation factor binding protein GGA1 | A | protein | 140 | Homo sapiens | Q9UJY5 (AlphaFold model) |
>1O3X_1 ADP-ribosylation factor binding protein GGA1 (chains A) NVIFEDEEKSKMLARLLKSSHPEDLRAANKLIKEMVQEDQKRMEKISKRVNAIEEVNNNV KLLTEMVMSHSQGGAAAGSSEDLMKELYQRCERMRPTLFRLASDTEDNDEALAEILQAND NLTQVINLYKQLVRGEEVNG
Molecular Mechanism of Membrane Recruitment of Gga by Arf in Lysosomal Protein Transport. Shiba, T., Kawasaki, M., Takatsu, H. et al. Nat Struct Biol (2003) 10:386-393. DOI 10.1038/nsb920 · PubMed
Other PDB entries of the same protein (UniProt Q9UJY5 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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