Alanine 31 proline mutant of rop protein, monoclinic form. Determined by X-ray diffraction at 1.9 Å resolution. Released 12 Sept 2002.
Explore 1GMG in 3D Show helices and sheets RCSB PDB PDBe
1GMG contains 4 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 3-26 | 24 | |
| α-helix | 31-54 | 24 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-26 | 23 | |
| α-helix | 31-54 | 24 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Regulatory protein rop | A, B | protein | 63 | ESCHERICHIA COLI | P03051 (AlphaFold model) |
>1GMG_1 REGULATORY PROTEIN ROP (chains A, B) MTKQEKTALNMARFIRSQTLTLLEKLNELDPDEQADICESLHDHADELYRSCLARFGDDG ENL
Structure Determination of a Small Protein Through a 23-Dimensional Molecular-Replacement Search. Glykos, N.M., Kokkinidis, M. Acta Crystallogr D Biol Crystallogr (2003) 59:709. DOI 10.1107/S0907444903002889 · PubMed
Other PDB entries of the same protein (UniProt P03051 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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