Crystal Structure of a Novel Alanine-Zipper Trimer at 1.7 A Resolution, V13A,L16A,V20A,L23A,V27A,M30A,V34A mutations. Determined by X-ray diffraction at 1.7 Å resolution. Released 17 Jun 2003.
Explore 1JCC in 3D Show helices and sheets RCSB PDB PDBe
1JCC 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 | 4-49 | 46 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-50 | 47 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Major outer membrane lipoprotein | A, B, C | protein | 56 | Escherichia coli | P69776 (AlphaFold model) |
>1JCC_1 MAJOR OUTER MEMBRANE LIPOPROTEIN (chains A, B, C) SSNAKIDQLSSDAQTANAKADQASNDANAARSDAQAAKDDAARANQRLDNMATKYR
| ID | Name | Formula | Copies |
|---|---|---|---|
| ZN | Zinc ion | Zn | 3 |
Zinc-Mediated Helix Capping in A Triple-Helical Protein. Liu, J., Dai, J., Lu, M. Biochemistry (2003) 42:5657-5664. DOI 10.1021/bi026828a · 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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