3O20: Cytochrome c

Electron transfer complexes:experimental mapping of the Redox-dependent Cytochrome C electrostatic surface. Determined by X-ray diffraction at 1.9 Å resolution. Released 25 Jan 2012.

Method: X-ray diffraction
Resolution: 1.9 Å
Organism: Equus caballus
Chains: 3
Atoms: 3,050
Mol. weight: 38.23 kDa
Ligands: HEC
Released: 25 Jan 2012

Explore 3O20 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3O20 contains 22 α-helices and 6 β-strands across 3 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: 8 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	3-13	11
α-helix	24-26	3
β-strand	39	1	1
α-helix	50-53	4
α-helix	57	1
β-strand	58	1	1
α-helix	59	1
α-helix	61-69	9
α-helix	71-74	4
α-helix	88-101	14

Chain B: 7 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	3-13	11
α-helix	24-26	3
α-helix	38	1
β-strand	39	1	2
α-helix	50-53	4
β-strand	58	1	2
α-helix	61-69	9
α-helix	71-74	4
α-helix	88-101	14

Chain C: 7 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	3-13	11
α-helix	24-26	3
α-helix	30-31	2
β-strand	39	1	3
α-helix	50-53	4
β-strand	58	1	3
α-helix	61-69	9
α-helix	71-74	4
α-helix	88-101	14

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cytochrome c	A, B, C	protein	105	Equus caballus	P00004 (AlphaFold model)

Sequence of entity 1 (A, B, C), FASTA

>3O20_1 Cytochrome c (chains A, B, C)
XGDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITW
KEETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE

Ligands and cofactors

ID	Name	Formula	Copies
HEC	Heme C	C34 H36 Fe N4 O4	3

Water and common crystallization additives (NO3) are not listed.

Primary citation

Nitrate as a probe of cytochrome c surface: crystallographic identification of crucial "hot spots" for protein-protein recognition. De March, M., Demitri, N., De Zorzi, R. et al. J Inorg Biochem (2014) 135:58-67. DOI 10.1016/j.jinorgbio.2014.02.015 · PubMed

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

6K9J 0.98 Å, 0.98 A three-dimensional structure of horse heart cytochrome C at 110K
8ZXR 1.6 Å, Crystal structure of Ssr1698 in complex with heme c
3O1Y 1.75 Å, Electron transfer complexes: Experimental mapping of the redox-dependent cytochrome c…
1WEJ 1.8 Å, IgG1 FAB fragment (of E8 antibody) complexed with horse cytochrome C at 1.8 a resolution
3WC8 1.8 Å, Dimeric horse cytochrome c obtained by refolding with desalting method
3WUI 1.8 Å, Dimeric horse cytochrome c formed by refolding from molten globule state
6K9I 1.8 Å, High-resolution three-dimensional structure of horse heart cytochrome C at room…
1HRC 1.9 Å, High-resolution three-dimensional structure of horse heart cytochrome C
5IY5 2.0 Å, Electron transfer complex of cytochrome c and cytochrome c oxidase at 2.0 angstrom…
1CRC 2.08 Å, Cytochrome C at low ionic strength
3NBT 2.1 Å, Crystal structure of trimeric cytochrome c from horse heart
4NFG 2.11 Å, K13R mutant of horse cytochrome c and yeast cytochrome c peroxidase complex

Browse structure collections

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