256B: Cytochrome B562

Improvement of the 2.5 Å resolution model of cytochrome B562 by redetermining the primary structure and using molecular graphics. Determined by X-ray diffraction at 1.4 Å resolution. Released 15 Jan 1991.

Method
X-ray diffraction
Resolution
1.4 Å
Organism
Escherichia coli
Chains
2
Atoms
1,923
Mol. weight
25.22 kDa
Ligands
HEM
Released
15 Jan 1991

Explore 256B in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

256B 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: 6 helices, 0 β-strands

ElementResiduesLengthSheet
α-helix3-1917
α-helix23-4018
α-helix46-483
α-helix56-8025
α-helix84-918
α-helix93-10513
Chain B: 6 helices, 0 β-strands
ElementResiduesLengthSheet
α-helix3-1917
α-helix23-4018
α-helix46-483
α-helix56-8025
α-helix84-929
α-helix94-10512

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cytochrome B562A, Bprotein106Escherichia coliP0ABE7 (AlphaFold model)
Sequence of entity 1 (A, B), FASTA
>256B_1 CYTOCHROME B562 (chains A, B)
ADLEDNMETLNDNLKVIEKADNAAQVKDALTKMRAAALDAQKATPPKLEDKSPDSPEMKD
FRHGFDILVGQIDDALKLANEGKVKEAQAAAEQLKTTRNAYHQKYR

Ligands and cofactors

IDNameFormulaCopies
HEMProtoporphyrin IX containing FEC34 H32 Fe N4 O42

Water and common crystallization additives (SO4) are not listed.

Primary citation

Improvement of the 2.5 A resolution model of cytochrome b562 by redetermining the primary structure and using molecular graphics. Lederer, F., Glatigny, A., Bethge, P.H. et al. J Mol Biol (1981) 148:427-448. DOI 10.1016/0022-2836(81)90185-6 · PubMed

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

Browse structure collections

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