5WO2: Chaperone Spy

Chaperone Spy bound to Casein Fragment (Casein un-modeled). Determined by X-ray diffraction at 1.77 Å resolution. Released 16 Aug 2017.

Method
X-ray diffraction
Resolution
1.77 Å
Organism
Escherichia coli
Chains
2
Atoms
1,669
Mol. weight
24.61 kDa
Ligands
ZN
Released
16 Aug 2017

Explore 5WO2 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

5WO2 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-helix30-323
α-helix36-4510
α-helix58-6811
α-helix75-839
α-helix86-10419
α-helix109-12012
Chain B: 4 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix36-4813
α-helix59-6810
α-helix75-10430
α-helix109-12113

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Periplasmic chaperone SpyA, Bprotein97Escherichia coliP77754 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>5WO2_1 Periplasmic chaperone Spy (chains A, B)
SFKDLNLTDAQKQQIREIMKGQRDQMKRPPLEERRAMHDIIASDTFDKVKAEAQIAKMEE
QRKANMLAHMETQNKIYNILTPEQKKQFNANFEKRLT

Ligands and cofactors

IDNameFormulaCopies
ZNZinc ionZn16

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:

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