Solution structure of the monocyte chemoattractant protein-1 dimer using heteronuclear, NMR, minimized average structure. Determined by solution NMR. Released 14 Oct 1996.
Explore 1DOM in 3D Show helices and sheets RCSB PDB PDBe
1DOM contains 2 α-helices and 12 β-strands across 2 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 |
|---|---|---|---|
| β-strand | 9-11 | 3 | 1 |
| β-strand | 27-28 | 2 | 2 |
| β-strand | 31 | 1 | 3 |
| β-strand | 40 | 1 | 3 |
| β-strand | 41-44 | 4 | 2 |
| β-strand | 50-53 | 4 | 2 |
| α-helix | 60-68 | 9 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| MCP-1 | A, B | protein | 76 | Homo sapiens | P13500 (AlphaFold model) |
>1DOM_1 MCP-1 (chains A, B) QPDAINAPVTCCYNFTNRKISVQRLASYRRITSSKCPKEAVIFKTIVAKEICADPKQKWV QDSMDHLDKQTQTPKT
Heteronuclear (1H, 13C, 15N) NMR assignments and solution structure of the monocyte chemoattractant protein-1 (MCP-1) dimer. Handel, T.M., Domaille, P.J. Biochemistry (1996) 35:6569-6584. DOI 10.1021/bi9602270 · 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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