3WC8: Cytochrome c

Dimeric horse cytochrome c obtained by refolding with desalting method. Determined by X-ray diffraction at 1.8 Å resolution. Released 11 Dec 2013.

Method
X-ray diffraction
Resolution
1.8 Å
Organism
Equus caballus
Chains
1
Atoms
976
Mol. weight
12.95 kDa
Ligands
HEC, PO4
Released
11 Dec 2013

Explore 3WC8 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3WC8 contains 10 α-helices and 2 β-strands across 1 chain. 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: 10 helices, 2 β-strands

ElementResiduesLengthSheet
α-helix3-1311
α-helix24-263
α-helix30-312
α-helix381
β-strand3911
α-helix50-545
α-helix571
β-strand5811
α-helix591
α-helix61-699
α-helix71-744
α-helix88-10114

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Cytochrome cAprotein104Equus caballusP00004 (AlphaFold model)
Sequence of entity 1 (A), FASTA
>3WC8_1 Cytochrome c (chains A)
GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWK
EETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE

Ligands and cofactors

IDNameFormulaCopies
HECHeme CC34 H36 Fe N4 O41
PO4Phosphate ionO4 P1

Water and common crystallization additives (PEG, PG4) are not listed.

Primary citation

Formation of Oligomeric Cytochrome c during Folding by Intermolecular Hydrophobic Interaction between N- and C-Terminal alpha-Helices. Parui, P.P., Deshpande, M.S., Nagao, S. et al. Biochemistry (2013) 52:8732-8744. DOI 10.1021/bi400986g · PubMed

Other PDB entries of the same protein (UniProt P00004 (AlphaFold model), which also has an AlphaFold model), best resolution first:

Browse structure collections

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