X-ray Structure of Macrophage Inflammatory Protein-1 alpha polymer. Determined by X-ray diffraction at 2.65 Å resolution. Released 3 Nov 2010.
Explore 2X69 in 3D Show helices and sheets RCSB PDB PDBe
2X69 contains 17 α-helices and 19 β-strands across 5 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 | 22-24 | 3 | |
| β-strand | 25-30 | 6 | 1 |
| α-helix | 31-32 | 2 | |
| β-strand | 40-44 | 5 | 1 |
| β-strand | 49-52 | 4 | 1 |
| α-helix | 57-67 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-8 | 2 | |
| β-strand | 9-11 | 3 | 2 |
| α-helix | 19-21 | 3 | |
| α-helix | 22-24 | 3 | |
| β-strand | 25-30 | 6 | 3 |
| α-helix | 31-32 | 2 | |
| β-strand | 40-44 | 5 | 3 |
| β-strand | 49-52 | 4 | 3 |
| α-helix | 57-67 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-11 | 3 | 2 |
| α-helix | 22-24 | 3 | |
| β-strand | 25-30 | 6 | 4 |
| β-strand | 40-44 | 5 | 4 |
| β-strand | 49-52 | 4 | 4 |
| α-helix | 57-68 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 7-8 | 2 | |
| β-strand | 9-11 | 3 | 5 |
| α-helix | 19-21 | 3 | |
| α-helix | 22-24 | 3 | |
| β-strand | 25-30 | 6 | 6 |
| β-strand | 40-44 | 5 | 6 |
| β-strand | 49-52 | 4 | 6 |
| α-helix | 57-67 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-11 | 3 | 5 |
| α-helix | 19-20 | 2 | |
| β-strand | 25-30 | 6 | 7 |
| α-helix | 31-32 | 2 | |
| β-strand | 40-44 | 5 | 7 |
| β-strand | 49-52 | 4 | 7 |
| α-helix | 57-68 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| C-C motif chemokine 3 | A, B, C, D, E | protein | 70 | HOMO SAPIENS | P10147 (AlphaFold model) |
>2X69_1 C-C MOTIF CHEMOKINE 3 (chains A, B, C, D, E) ASLAADTPTACCFSYTSRQIPQNFIADYFETSSQCSKPGVIFLTKRSRQVCADPSEEWVQ KYVSDLELSA
Polymerization of Mip-1 Chemokine (Ccl3 and Ccl4) and Clearance of Mip-1 by Insulin-Degrading Enzyme. Ren, M., Guo, Q., Guo, L. et al. EMBO J (2010) 29:3952. DOI 10.1038/EMBOJ.2010.256 · PubMed
Other PDB entries of the same protein (UniProt P10147 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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