6DYF: Soluble cytochrome b562

Cu(II)-bound structure of the engineered cyt cb562 variant, CH3Y. Determined by X-ray diffraction at 1.1 Å resolution. Released 24 Apr 2019.

Method
X-ray diffraction
Resolution
1.1 Å
Organism
Escherichia coli
Chains
2
Atoms
2,259
Mol. weight
25.29 kDa
Ligands
HEC, CU
Released
24 Apr 2019

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

Secondary structure: helices and β-sheets

6DYF contains 12 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: 7 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-1917
α-helix23-4018
α-helix44-452
α-helix46-483
α-helix56-8025
α-helix84-929
α-helix95-10511
Chain B: 5 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix3-1917
α-helix23-4018
α-helix46-483
α-helix56-8025
α-helix84-10522

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Soluble cytochrome b562A, Bprotein106Escherichia coliP0ABE7 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>6DYF_1 Soluble cytochrome b562 (chains A, B)
ADLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMWD
FRHGFDHLVYHIDDALKLANEGKVKEAQAAAEQLKCHCNACHQKYR

Ligands and cofactors

IDNameFormulaCopies
HECHeme CC34 H36 Fe N4 O42
CUCopper (II) ionCu1

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

Primary citation

An efficient, step-economical strategy for the design of functional metalloproteins. Rittle, J., Field, M.J., Green, M.T. et al. Nat Chem (2019) 11:434-441. DOI 10.1038/s41557-019-0218-9 · PubMed

Other PDB entries of the same protein (UniProt P0ABE7 (AlphaFold model), which also has an AlphaFold model), best resolution first:

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