X-ray structure of the small G protein Rab11a in complex with GDP. Determined by X-ray diffraction at 1.98 Å resolution. Released 8 Jan 2004.
Explore 1OIV in 3D Show helices and sheets RCSB PDB PDBe
1OIV contains 14 α-helices and 12 β-strands across 2 chains. 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 |
|---|---|---|---|
| β-strand | 10-17 | 8 | 1 |
| α-helix | 24-33 | 10 | |
| β-strand | 46-55 | 10 | 1 |
| β-strand | 58-67 | 10 | 1 |
| α-helix | 74-81 | 8 | |
| β-strand | 84-92 | 9 | 1 |
| α-helix | 96-100 | 5 | |
| α-helix | 102-112 | 11 | |
| β-strand | 118-124 | 7 | 1 |
| α-helix | 129-131 | 3 | |
| α-helix | 136-146 | 11 | |
| β-strand | 149-152 | 4 | 1 |
| α-helix | 161-172 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-17 | 8 | 1 |
| α-helix | 24-33 | 10 | |
| β-strand | 46-55 | 10 | 1 |
| β-strand | 58-67 | 10 | 1 |
| α-helix | 74-81 | 8 | |
| β-strand | 86-92 | 7 | 1 |
| α-helix | 96-100 | 5 | |
| α-helix | 102-112 | 11 | |
| β-strand | 118-124 | 7 | 1 |
| α-helix | 126-131 | 6 | |
| α-helix | 136-145 | 10 | |
| β-strand | 149-152 | 4 | 1 |
| α-helix | 161-172 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ras-related protein rab-11A | A, B | protein | 191 | HOMO SAPIENS | P62491 (AlphaFold model) |
>1OIV_1 RAS-RELATED PROTEIN RAB-11A (chains A, B) MRGSHHHHHHGIPLPGRAMGTRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKS TIGVEFATRSIQVDGKTIKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHLTYENV ERWLKELRDHADSNIVIMLVGNKSDLRHLRAVPTDEARAFAEKNGLSFIETSALDSTNVE AAFQTILTEIY
| ID | Name | Formula | Copies |
|---|---|---|---|
| GDP | Guanosine-5'-diphosphate | C10 H15 N5 O11 P2 | 2 |
Water and common crystallization additives (EDO, SO4) are not listed.
The Structural Gdp/GTP Cycle of Rab11 Reveals a Novel Interface Involved in the Dynamics of Recycling Endosomes. Pasqualato, S., Senic-Matuglia, F., Renault, L. et al. J Biol Chem (2004) 279:11480. DOI 10.1074/JBC.M310558200 · PubMed
Other PDB entries of the same protein (UniProt P62491 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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