Structure of HIS15ASP hpr after hydrolysis of ringed species. Determined by X-ray diffraction at 1.8 Å resolution. Released 17 May 2000.
Explore 1CM2 in 3D Show helices and sheets RCSB PDB PDBe
1CM2 contains 3 α-helices and 4 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 |
|---|---|---|---|
| β-strand | 2-7 | 6 | 1 |
| α-helix | 16-26 | 11 | |
| β-strand | 32-37 | 6 | 1 |
| β-strand | 40-43 | 4 | 1 |
| α-helix | 47-50 | 4 | |
| β-strand | 60-66 | 7 | 1 |
| α-helix | 70-83 | 14 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Histidine-containing protein | A | protein | 85 | Escherichia coli | P0AA04 (AlphaFold model) |
>1CM2_1 HISTIDINE-CONTAINING PROTEIN (chains A) MFQQEVTITAPNGLDTRPAAQFVKEAKGFTSEITVTSNGKSASAKSLFKLQTLGLTQGTV VTISAEGEDEQKAVEHLVKLMAELE
The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli Phosphoenolpyruvate:Sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization. Napper, S., Delbaere, L.T., Waygood, E.B. J Biol Chem (1999) 274:21776-21782. DOI 10.1074/jbc.274.31.21776 · PubMed
Other PDB entries of the same protein (UniProt P0AA04 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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