5EKI: Truncated CCL21

Crystal Structure of Truncated CCL21. Determined by X-ray diffraction at 1.9 Å resolution. Released 5 Oct 2016.

Method
X-ray diffraction
Resolution
1.9 Å
Organism
Homo sapiens
Chains
6
Atoms
3,639
Mol. weight
53.67 kDa
Released
5 Oct 2016

Explore 5EKI in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5EKI contains 17 α-helices and 32 β-strands across 6 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: 2 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand811
α-helix19-213
β-strand22-2872
β-strand38-4362
β-strand51-5332
α-helix58-6710
β-strand7413
Chain B: 2 helices, 7 β-strands
ElementResiduesLengthSheet
β-strand814
α-helix19-213
β-strand22-2875
β-strand3116
β-strand3416
β-strand38-4365
β-strand51-5335
α-helix58-6710
β-strand7417
Chain C: 4 helices, 5 β-strands
ElementResiduesLengthSheet
β-strand817
α-helix19-213
β-strand22-2878
α-helix30-323
β-strand38-4368
α-helix49-502
β-strand51-5338
α-helix58-6710
β-strand7419
Chain D: 3 helices, 5 β-strands
ElementResiduesLengthSheet
β-strand813
α-helix16-183
α-helix19-213
β-strand22-28710
β-strand38-43610
β-strand51-53310
α-helix58-6710
β-strand74111
Chains E and F: 3 helices, 5 β-strands
ElementResiduesLengthSheet
β-strand8111
α-helix19-213
β-strand22-28712
β-strand38-43612
α-helix49-502
β-strand51-53312
α-helix58-6710
β-strand7414

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
C-C motif chemokine 21A, B, C, D, E, Fprotein79Homo sapiensO00585 (AlphaFold model)
Sequence of entity 1 (A, B, C, D, E, F), FASTA
>5EKI_1 C-C motif chemokine 21 (chains A, B, C, D, E, F)
SDGGAQDCCLKYSQRKIPAKVVRSYRKQEPSLGCSIPAILFLPRKRSQAELCADPKELWV
QQLMQHLDKTPSPQKPAQG

Primary citation

Crystallographic Structure of Truncated CCL21 and the Putative Sulfotyrosine-Binding Site. Smith, E.W., Lewandowski, E.M., Moussouras, N.A. et al. Biochemistry (2016) 55:5746-5753. DOI 10.1021/acs.biochem.6b00304 · PubMed

Other PDB entries of the same protein (UniProt O00585 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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