NMR structure of human mip-1A D26A, minimized average structure. Determined by solution NMR. Released 22 Jul 1999.
Explore 1B53 in 3D Show helices and sheets RCSB PDB PDBe
1B53 contains 4 α-helices and 0 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 |
|---|---|---|---|
| α-helix | 21-23 | 3 | |
| α-helix | 58-63 | 6 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Mip-1A | A, B | protein | 69 | Homo sapiens | P10147 (AlphaFold model) |
>1B53_1 MIP-1A (chains A, B) SLAADTPTACCFSYTSRQIPQNFIAAYFETSSQCSKPGVIFLTKRSRQVCADPSEEWVQK YVSDLELSA
Identification of amino acid residues critical for aggregation of human CC chemokines macrophage inflammatory protein (MIP)-1alpha, MIP-1beta, and RANTES. Characterization of active disaggregated chemokine variants. Czaplewski, L.G., McKeating, J., Craven, C.J. et al. J Biol Chem (1999) 274:16077-16084. DOI 10.1074/jbc.274.23.16077 · PubMed
Other PDB entries of the same protein (UniProt P10147 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 1B53 directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.