6STK: CC-chemokine 5 (CCL5) E66S mutation

Crystal structure of the CC-chemokine 5 (CCL5) E66S mutation. Determined by X-ray diffraction at 1.52 Å resolution. Released 2 Sept 2020.

Method
X-ray diffraction
Resolution
1.52 Å
Organism
Homo sapiens
Chains
2
Atoms
1,194
Mol. weight
15.79 kDa
Released
2 Sept 2020

Explore 6STK in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6STK contains 8 α-helices and 9 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: 4 helices, 5 β-strands

ElementResiduesLengthSheet
β-strand611
β-strand8-1142
α-helix18-203
α-helix21-233
β-strand24-2963
α-helix30-312
β-strand39-4353
β-strand48-5143
α-helix56-6510
Chain B: 4 helices, 4 β-strands
ElementResiduesLengthSheet
β-strand7-1042
α-helix18-203
α-helix21-233
β-strand24-2961
α-helix30-312
β-strand39-4351
β-strand48-5141
α-helix56-6510

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
C-C motif chemokine 5A, Bprotein68Homo sapiensP13501 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6STK_1 C-C motif chemokine 5 (chains A, B)
SPYSSDTTPCCFAYIARPLPRAHIKEYFYTSGKCSNPAVVFVTRKNRQVCANPEKKWVRE
YINSLSMS

Primary citation

Structural characterization of anti-CCL5 activity of the tick salivary protein evasin-4. Denisov, S.S., Ramirez-Escudero, M., Heinzmann, A.C.A. et al. J Biol Chem (2020) 295:14367-14378. DOI 10.1074/jbc.RA120.013891 · PubMed

Other PDB entries of the same protein (UniProt P13501 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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