Crystal structure of human monocyte chemotactic protein-2. Determined by X-ray diffraction at 2.0 Å resolution. Released 6 Dec 2000.
Explore 1ESR in 3D Show helices and sheets RCSB PDB PDBe
1ESR contains 2 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 | 22-24 | 3 | |
| β-strand | 25-30 | 6 | 1 |
| β-strand | 41-45 | 5 | 1 |
| β-strand | 50-53 | 4 | 1 |
| α-helix | 58-73 | 16 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Monocyte chemotactic protein 2 | A | protein | 76 | Homo sapiens | P80075 (AlphaFold model) |
>1ESR_1 MONOCYTE CHEMOTACTIC PROTEIN 2 (chains A) QPDSVSIPITCCFNVINRKIPIQRLESYTRITNIQCPKEAVIFKTQRGKEVCADPKERWV RDSMKHLDQIFQNLKP
Complete crystal structure of monocyte chemotactic protein-2, a CC chemokine that interacts with multiple receptors. Blaszczyk, J., Coillie, E.V., Proost, P. et al. Biochemistry (2000) 39:14075-14081. DOI 10.1021/bi0009340 · PubMed
Other PDB entries of the same protein (UniProt P80075 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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