Mad structure of the periplasmique domain of the Escherichia coli PAL protein. Determined by X-ray diffraction at 1.93 Å resolution. Released 13 Feb 2004.
Explore 1OAP in 3D Show helices and sheets RCSB PDB PDBe
1OAP contains 6 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 | 49-51 | 3 | 1 |
| α-helix | 58-60 | 3 | |
| α-helix | 61-63 | 3 | |
| α-helix | 64-75 | 12 | |
| β-strand | 82-86 | 5 | 1 |
| α-helix | 94-113 | 20 | |
| α-helix | 119-121 | 3 | |
| β-strand | 122-126 | 5 | 1 |
| α-helix | 139-145 | 7 | |
| β-strand | 147-151 | 5 | 1 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Peptidoglycan-associated lipoprotein | A | protein | 109 | ESCHERICHIA COLI | P0A912 (AlphaFold model) |
>1OAP_1 PEPTIDOGLYCAN-ASSOCIATED LIPOPROTEIN (chains A) LQQNNIVYFDLDKYDIRSDFAQMLDAHANFLRSNPSYKVTVEGHADERGTPEYNISLGER RANAVKMYLQGKGVSADQISIVSYGKEKPAVLGHDEAAYSKNRRAVLVY
Crystallization and preliminary crystallographic study of the peptidoglycan-associated lipoprotein from Escherichia coli. Abergel, C., Walburger, A., Chenivesse, S. et al. Acta Crystallogr D Biol Crystallogr (2001) 57:317-319. DOI 10.1107/s0907444900019739 · PubMed
Other PDB entries of the same protein (UniProt P0A912 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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