Amino terminal domain of enzyme I from escherichia coli NMR, restrained regularized mean structure. Determined by solution NMR. Released 7 Jan 1998.
Explore 1EZA in 3D Show helices and sheets RCSB PDB PDBe
1EZA contains 13 α-helices and 10 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 | 8 | 1 | 1 |
| β-strand | 12-15 | 4 | 2 |
| β-strand | 16-18 | 3 | 1 |
| α-helix | 22-24 | 3 | |
| α-helix | 29-32 | 4 | |
| α-helix | 33-64 | 32 | |
| α-helix | 67-80 | 14 | |
| α-helix | 83-95 | 13 | |
| α-helix | 100-116 | 17 | |
| α-helix | 121-141 | 21 | |
| α-helix | 149-151 | 3 | |
| β-strand | 156-160 | 5 | 1 |
| α-helix | 165-170 | 6 | |
| β-strand | 176-181 | 6 | 1 |
| β-strand | 182 | 1 | 3 |
| α-helix | 189-197 | 9 | |
| β-strand | 201-202 | 2 | 1 |
| β-strand | 204 | 1 | 3 |
| α-helix | 208-210 | 3 | |
| β-strand | 217-220 | 4 | 2 |
| β-strand | 227-229 | 3 | 2 |
| α-helix | 233-251 | 19 | |
| α-helix | 253-255 | 3 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Enzyme I | A | protein | 259 | Escherichia coli | P08839 (AlphaFold model) |
>1EZA_1 ENZYME I (chains A) MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTK AGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDD EYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFI TDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMR AVQEQVASEKAELAKLKDR
Solution structure of the 30 kDa N-terminal domain of enzyme I of the Escherichia coli phosphoenolpyruvate:sugar phosphotransferase system by multidimensional NMR. Garrett, D.S., Seok, Y.J., Liao, D.I. et al. Biochemistry (1997) 36:2517-2530. DOI 10.1021/bi962924y · PubMed
Other PDB entries of the same protein (UniProt P08839 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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