Crystal structure of CXCL13. Determined by X-ray diffraction at 1.88 Å resolution. Released 7 Oct 2020.
Explore 7JNY in 3D Show helices and sheets RCSB PDB PDBe
7JNY contains 3 α-helices and 5 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 |
|---|---|---|---|
| β-strand | 1-4 | 4 | 1 |
| α-helix | 9-11 | 3 | |
| β-strand | 17 | 1 | 1 |
| α-helix | 23-25 | 3 | |
| β-strand | 26-32 | 7 | 1 |
| β-strand | 42-47 | 6 | 1 |
| β-strand | 52-55 | 4 | 1 |
| α-helix | 60-71 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| C-X-C motif chemokine 13 | A | protein | 88 | Homo sapiens | O43927 (AlphaFold model) |
>7JNY_1 C-X-C motif chemokine 13 (chains A) MVLEVYYTSLRCRCVQESSVFIPRRFIDRIQILPRGNGCPRKEIIVWKKNKSIVCVDPQA EWIQRMMEVLRKRSSSTLPVPVFKRKIP
The N-terminal length and side-chain composition of CXCL13 affect crystallization, structure and functional activity. Rosenberg Jr., E.M., Herrington, J., Rajasekaran, D. et al. Acta Crystallogr D Struct Biol (2020) 76:1033-1049. DOI 10.1107/S2059798320011687 · PubMed
Other PDB entries of the same protein (UniProt O43927 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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