Monocyte chemoattractant protein 1, I-form. Determined by X-ray diffraction at 2.4 Å resolution. Released 12 Mar 1997.
Explore 1DOL in 3D Show helices and sheets RCSB PDB PDBe
1DOL contains 3 α-helices and 3 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 |
|---|---|---|---|
| α-helix | 4-6 | 3 | |
| α-helix | 22-24 | 3 | |
| β-strand | 25-31 | 7 | 1 |
| β-strand | 40-45 | 6 | 1 |
| β-strand | 50-53 | 4 | 1 |
| α-helix | 58-67 | 10 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Monocyte chemoattractant protein 1 | A | protein | 77 | Homo sapiens | P13500 (AlphaFold model) |
>1DOL_1 MONOCYTE CHEMOATTRACTANT PROTEIN 1 (chains A) MQPDAINAPVTCCYNFTNRKISVQRLASYRRITSSKCPKEAVIFKTIVAKEICADPKQKW VQDSMDHLDKQTQTPKT
The structure of MCP-1 in two crystal forms provides a rare example of variable quaternary interactions. Lubkowski, J., Bujacz, G., Boque, L. et al. Nat Struct Biol (1997) 4:64-69. DOI 10.1038/nsb0197-64 · PubMed
Other PDB entries of the same protein (UniProt P13500 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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