5WNW: Chaperone Spy

Chaperone Spy bound to Im7 6-45 ensemble. Determined by X-ray diffraction at 1.79 Å resolution. Released 16 Aug 2017.

Method
X-ray diffraction
Resolution
1.79 Å
Organism
Escherichia coli
Chains
3
Atoms
1,765
Mol. weight
28.45 kDa
Ligands
ZN
Released
16 Aug 2017

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

Secondary structure: helices and β-sheets

5WNW contains 10 α-helices and 0 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: 6 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix29-324
α-helix36-4611
α-helix58-6811
α-helix75-8410
α-helix86-10419
α-helix109-12012
Chain B: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix36-4611
α-helix59-6810
α-helix75-10430
α-helix109-12113

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Periplasmic chaperone SpyA, Bprotein97Escherichia coliP77754 (AlphaFold model)
Colicin-E7 immunity proteinCprotein40Escherichia coliQ03708 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5WNW_1 Periplasmic chaperone Spy (chains A, B)
SFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEE
QRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLT
Sequence of entity 2 (C), FASTA
>5WNW_2 Colicin-E7 immunity protein (chains C)
SISDYTEAEFVQLLKEIEKENVAATDDVLDVLLEHFVKIT

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn8

Water and common crystallization additives (CL, IMD) are not listed.

Primary citation

Visualizing chaperone-assisted protein folding. Horowitz, S., Salmon, L., Koldewey, P. et al. Nat Struct Mol Biol (2016) 23:691-697. DOI 10.1038/nsmb.3237 · PubMed

Other PDB entries of the same protein (UniProt P77754 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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