Human macrophage inflammatory protein-1 alpha L3M_V63M. Determined by X-ray diffraction at 2.65 Å resolution. Released 27 Oct 2010.
Explore 3KBX in 3D Show helices and sheets RCSB PDB PDBe
3KBX contains 19 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 | 19-21 | 3 | |
| α-helix | 22-24 | 3 | |
| β-strand | 25-30 | 6 | 1 |
| β-strand | 40-44 | 5 | 1 |
| β-strand | 49-52 | 4 | 1 |
| α-helix | 57-67 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-11 | 3 | 2 |
| α-helix | 19-20 | 2 | |
| 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 | 19-21 | 3 | |
| α-helix | 22-24 | 3 | |
| β-strand | 25-30 | 6 | 4 |
| α-helix | 31-32 | 2 | |
| β-strand | 40-44 | 5 | 4 |
| β-strand | 49-52 | 4 | 4 |
| α-helix | 57-68 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8 | 1 | |
| 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 | 19-21 | 3 | |
| α-helix | 22-24 | 3 | |
| 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 | 57-67 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| CCL3 | A, B, C, D, E | protein | 70 | Homo sapiens | P10147 (AlphaFold model) |
>3KBX_1 CCL3 (chains A, B, C, D, E) ASMAADTPTACCFSYTSRQIPQNFIADYFETSSQCSKPGVIFLTKRSRQVCADPSEEWVQ KYMSDLELSA
Structural basis for the oligomerization of macrophage inflammatory protein-1 alpha. Guo, Q., Ren, M., Tang, W.-J. To be published.
Other PDB entries of the same protein (UniProt P10147 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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