Crystal Structure of mouse Rab27b bound to GDP in monoclinic space group. Determined by X-ray diffraction at 2.8 Å resolution. Released 1 May 2007.
Explore 2IEZ in 3D Show helices and sheets RCSB PDB PDBe
2IEZ contains 28 α-helices and 29 β-strands across 4 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 | 9-15 | 7 | 1 |
| α-helix | 22-30 | 9 | |
| β-strand | 37-53 | 17 | 1 |
| β-strand | 66-76 | 11 | 1 |
| α-helix | 80-89 | 10 | |
| β-strand | 94-100 | 7 | 1 |
| α-helix | 105-115 | 11 | |
| α-helix | 126 | 1 | |
| β-strand | 127-133 | 7 | 1 |
| α-helix | 138-140 | 3 | |
| α-helix | 146-153 | 8 | |
| β-strand | 159-161 | 3 | 1 |
| β-strand | 163 | 1 | 2 |
| β-strand | 168 | 1 | 2 |
| α-helix | 170-187 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-15 | 8 | 1 |
| α-helix | 22-30 | 9 | |
| β-strand | 37-50 | 14 | 1 |
| β-strand | 69-76 | 8 | 1 |
| α-helix | 78-89 | 12 | |
| β-strand | 94-100 | 7 | 1 |
| α-helix | 104-114 | 11 | |
| α-helix | 117-119 | 3 | |
| β-strand | 127-133 | 7 | 1 |
| α-helix | 138-140 | 3 | |
| α-helix | 145-155 | 11 | |
| β-strand | 159-161 | 3 | 1 |
| α-helix | 170-187 | 18 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 12-15 | 4 | 3 |
| α-helix | 22-30 | 9 | |
| β-strand | 37-53 | 17 | 4 |
| β-strand | 66-76 | 11 | 4 |
| α-helix | 78-89 | 12 | |
| β-strand | 94-100 | 7 | 3 |
| α-helix | 104-113 | 10 | |
| α-helix | 125-126 | 2 | |
| β-strand | 127-133 | 7 | 3 |
| α-helix | 145-153 | 9 | |
| β-strand | 159-161 | 3 | 3 |
| β-strand | 163 | 1 | 5 |
| β-strand | 168 | 1 | 5 |
| α-helix | 170-186 | 17 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 8-15 | 8 | 4 |
| α-helix | 22-29 | 8 | |
| β-strand | 37-45 | 9 | 4 |
| β-strand | 72-73 | 2 | 3 |
| β-strand | 74-76 | 3 | 4 |
| α-helix | 79-89 | 11 | |
| β-strand | 94-100 | 7 | 4 |
| α-helix | 104-115 | 12 | |
| α-helix | 117-119 | 3 | |
| α-helix | 126 | 1 | |
| β-strand | 127-133 | 7 | 4 |
| α-helix | 138-140 | 3 | |
| α-helix | 145-153 | 9 | |
| β-strand | 159-161 | 3 | 4 |
| α-helix | 170-187 | 18 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Ras-related protein Rab-27B | A, B, H, I | protein | 220 | Mus musculus | Q99P58 (AlphaFold model) |
>2IEZ_1 Ras-related protein Rab-27B (chains A, B, H, I) GSMTDGDYDYLIKLLALGDSGVGKTTFLYRYTDNKFNPKFITTVGIDFREKRVVYDTQGA DGASGKAFKVHLQLWDTAGLERFRSLTTAFFRDAMGFLLMFDLTSQQSFLNVRNWMSQLQ ANAYCENPDIVLIGNKADLPDQREVNERQARELAEKYGIPYFETSAATGQNVEKSVETLL DLIMKRMEKCVEKTQVPDTVNGGNSGKLDGEKPAEKKCAC
Structure of the small GTPase Rab27b shows an unexpected swapped dimer. Chavas, L.M.G., Torii, S., Kamikubo, H. et al. Acta Crystallogr D Biol Crystallogr (2007) 63:769-779. DOI 10.1107/S0907444907019725 · PubMed
Other PDB entries of the same protein (UniProt Q99P58 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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