4RSZ: Cytochrome c

The X-ray structure of the Primary Adduct formed in the Reaction between Cisplatin and Cytochrome c. Determined by X-ray diffraction at 2.19 Å resolution. Released 14 Jan 2015.

Method: X-ray diffraction
Resolution: 2.19 Å
Organism: Equus caballus
Chains: 6
Atoms: 5,421
Mol. weight: 76.76 kDa
Ligands: HEC, CPT
Released: 14 Jan 2015

Explore 4RSZ in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

4RSZ contains 41 α-helices and 12 β-strands across 6 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, 2 β-strands

Element	Residues	Length	Sheet
α-helix	3-13	11
α-helix	24-26	3
β-strand	39	1	1
α-helix	50-54	5
β-strand	58	1	1
α-helix	61-69	9
α-helix	71-74	4
α-helix	88-101	14

Chains B, C, D, E and F: 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	2
α-helix	50-54	5
β-strand	58	1	2
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, D, E, F	protein	104	Equus caballus	P00004 (AlphaFold model)

Sequence of entity 1 (A, B, C, D, E, F), FASTA

>4RSZ_1 Cytochrome c (chains A, B, C, D, E, F)
GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWK
EETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE

Ligands and cofactors

ID	Name	Formula	Copies
HEC	Heme C	C34 H36 Fe N4 O4	6
CPT	Cisplatin	Cl2 H6 N2 Pt	5

Water and common crystallization additives (NO3, SO4) are not listed.

Primary citation

The X-ray structure of the primary adducts formed in the reaction between cisplatin and cytochrome c. Ferraro, G., Messori, L., Merlino, A. Chem Commun (Camb) (2015) 51:2559-2561. DOI 10.1039/c4cc09056j · 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
3O20 1.9 Å, Electron transfer complexes:experimental mapping of the Redox-dependent 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

Browse structure collections

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