Solution structure of the alternative conformation of XCL1/Lymphotactin. Determined by solution NMR. Released 11 Mar 2008.
Explore 2JP1 in 3D Show helices and sheets RCSB PDB PDBe
2JP1 contains 0 α-helices and 8 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 |
|---|---|---|---|
| β-strand | 11-15 | 5 | 1 |
| β-strand | 25-31 | 7 | 1 |
| β-strand | 34-40 | 7 | 1 |
| β-strand | 44-51 | 8 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 10-15 | 6 | 2 |
| β-strand | 25-31 | 7 | 2 |
| β-strand | 34-41 | 8 | 2 |
| β-strand | 44-51 | 8 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Lymphotactin | A, B | protein | 93 | Homo sapiens | P47992 (AlphaFold model) |
>2JP1_1 Lymphotactin (chains A, B) VGSEVSDKRTCVSLTTQRLPVSRIKTYTITEGSLRAVIFITKRGLKVCADPQATWVRDVV RSMDRKSNTRNNMIQTKPTGTQQSTNTAVTLTG
Interconversion between two unrelated protein folds in the lymphotactin native state. Tuinstra, R.L., Peterson, F.C., Kutlesa, S. et al. Proc Natl Acad Sci U S A (2008) 105:5057-5062. DOI 10.1073/pnas.0709518105 · PubMed
Other PDB entries of the same protein (UniProt P47992 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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