Crystal structure of Rab8 in its active GppNHp-bound form. Determined by X-ray diffraction at 1.55 Å resolution. Released 9 Oct 2013.
Explore 4LHW in 3D Show helices and sheets RCSB PDB PDBe
4LHW contains 43 α-helices and 42 β-strands across 5 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 | 7-14 | 8 | 1 |
| α-helix | 21-30 | 10 | |
| β-strand | 38 | 1 | 2 |
| β-strand | 43-52 | 10 | 1 |
| β-strand | 55-64 | 10 | 1 |
| α-helix | 73-78 | 6 | |
| β-strand | 83-89 | 7 | 1 |
| α-helix | 93-97 | 5 | |
| α-helix | 99-109 | 11 | |
| β-strand | 115-121 | 7 | 1 |
| α-helix | 126-128 | 3 | |
| α-helix | 133-143 | 11 | |
| β-strand | 146-149 | 4 | 1 |
| β-strand | 151 | 1 | 3 |
| β-strand | 156 | 1 | 3 |
| α-helix | 158-174 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-14 | 8 | 4 |
| α-helix | 21-30 | 10 | |
| β-strand | 43-52 | 10 | 4 |
| β-strand | 55-64 | 10 | 4 |
| α-helix | 68-70 | 3 | |
| α-helix | 71-76 | 6 | |
| β-strand | 83-89 | 7 | 4 |
| α-helix | 93-97 | 5 | |
| α-helix | 99-109 | 11 | |
| β-strand | 115-121 | 7 | 4 |
| α-helix | 126-128 | 3 | |
| α-helix | 133-143 | 11 | |
| β-strand | 146-149 | 4 | 4 |
| β-strand | 151 | 1 | 5 |
| β-strand | 156 | 1 | 5 |
| α-helix | 158-174 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-15 | 9 | 6 |
| α-helix | 21-30 | 10 | |
| β-strand | 34 | 1 | 2 |
| α-helix | 37-40 | 4 | |
| β-strand | 43-52 | 10 | 6 |
| β-strand | 55-64 | 10 | 6 |
| α-helix | 68-70 | 3 | |
| α-helix | 71-74 | 4 | |
| α-helix | 75-77 | 3 | |
| β-strand | 83-89 | 7 | 6 |
| α-helix | 93-97 | 5 | |
| α-helix | 99-109 | 11 | |
| β-strand | 115-121 | 7 | 6 |
| α-helix | 126-128 | 3 | |
| α-helix | 133-143 | 11 | |
| β-strand | 146-149 | 4 | 6 |
| β-strand | 151 | 1 | 7 |
| β-strand | 156 | 1 | 7 |
| α-helix | 158-175 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-14 | 8 | 8 |
| α-helix | 21-30 | 10 | |
| α-helix | 37-40 | 4 | |
| β-strand | 43-52 | 10 | 8 |
| β-strand | 55-64 | 10 | 8 |
| α-helix | 68-70 | 3 | |
| α-helix | 71-75 | 5 | |
| β-strand | 83-89 | 7 | 8 |
| α-helix | 93-97 | 5 | |
| α-helix | 99-109 | 11 | |
| β-strand | 115-121 | 7 | 8 |
| α-helix | 126-128 | 3 | |
| α-helix | 133-143 | 11 | |
| β-strand | 146-149 | 4 | 8 |
| β-strand | 151 | 1 | 9 |
| β-strand | 156 | 1 | 9 |
| α-helix | 158-173 | 16 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 7-14 | 8 | 10 |
| α-helix | 21-30 | 10 | |
| β-strand | 43-52 | 10 | 10 |
| β-strand | 55-64 | 10 | 10 |
| α-helix | 68-70 | 3 | |
| α-helix | 71-74 | 4 | |
| α-helix | 75-77 | 3 | |
| β-strand | 83-89 | 7 | 10 |
| α-helix | 93-97 | 5 | |
| α-helix | 99-108 | 10 | |
| β-strand | 115-121 | 7 | 10 |
| α-helix | 126-128 | 3 | |
| α-helix | 133-143 | 11 | |
| β-strand | 146-149 | 4 | 10 |
| β-strand | 151 | 1 | 11 |
| β-strand | 156 | 1 | 11 |
| α-helix | 158-175 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ras-related protein Rab-8A | A, B, C, D, E | protein | 174 | Homo sapiens | P61006 (AlphaFold model) |
>4LHW_1 Ras-related protein Rab-8A (chains A, B, C, D, E) GSHDYLFKLLLIGDSGVGKTCVLFRFSEDAFNSTFISTIGIDFKIRTIELDGKRIKLQIW DTAGQERFRTITTAYYRGAMGIMLVYDITNEKSFDNIRNWIRNIEEHASADVEKMILGNK CDVNDKRQVSKERGEKLALDYGIKFMETSAKANINVENAFFTLARDIKAKMDKK
| ID | Name | Formula | Copies |
|---|---|---|---|
| GNP | Phosphoaminophosphonic acid-guanylate ester | C10 H17 N6 O13 P3 | 5 |
| MG | Magnesium ion | Mg | 5 |
Water and common crystallization additives (MPD) are not listed.
Intermediates in the Guanine Nucleotide Exchange Reaction of Rab8 Protein Catalyzed by Guanine Nucleotide Exchange Factors Rabin8 and GRAB. Guo, Z., Hou, X., Goody, R.S. et al. J Biol Chem (2013) 288:32466-32474. DOI 10.1074/jbc.M113.498329 · PubMed
Other PDB entries of the same protein (UniProt P61006 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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