2JP1: Alternative conformation of XCL1/Lymphotactin

Solution structure of the alternative conformation of XCL1/Lymphotactin. Determined by solution NMR. Released 11 Mar 2008.

Method
Solution NMR
Organism
Homo sapiens
Chains
2
Atoms
930
Mol. weight
20.57 kDa
Released
11 Mar 2008

Explore 2JP1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 0 helices, 4 β-strands

ElementResiduesLengthSheet
β-strand11-1551
β-strand25-3171
β-strand34-4071
β-strand44-5181
Chain B: 0 helices, 4 β-strands
ElementResiduesLengthSheet
β-strand10-1562
β-strand25-3172
β-strand34-4182
β-strand44-5182

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
LymphotactinA, Bprotein93Homo sapiensP47992 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>2JP1_1 Lymphotactin (chains A, B)
VGSEVSDKRTCVSLTTQRLPVSRIKTYTITEGSLRAVIFITKRGLKVCADPQATWVRDVV
RSMDRKSNTRNNMIQTKPTGTQQSTNTAVTLTG

Primary citation

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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