Crystal Structure of a Novel Alanine-Zipper Trimer at 1.3 A Resolution, I6A,L9A,V13A,L16A,V20A,L23A,V27A,M30A,V34A,L48A,M51A mutations. Determined by X-ray diffraction at 1.3 Å resolution. Released 17 Jun 2003.
Explore 1JCD in 3D Show helices and sheets RCSB PDB PDBe
1JCD contains 3 α-helices and 0 β-strands across 3 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 | 4-50 | 47 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-51 | 48 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Major outer membrane lipoprotein | A, B, C | protein | 52 | Escherichia coli | P69776 (AlphaFold model) |
>1JCD_1 MAJOR OUTER MEMBRANE LIPOPROTEIN (chains A, B, C) SSNAKADQASSDAQTANAKADQASNDANAARSDAQAAKDDAARANQRADNAA
An Alanine-Zipper Structure Determined by Long Range Intermolecular Interactions. Liu, J., Lu, M. J Biol Chem (2002) 277:48708-48713. DOI 10.1074/jbc.M208773200 · PubMed
Other PDB entries of the same protein (UniProt P69776 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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