6SUV: Cytochrome c

Horse cytochrome c complexed by octa-anionic calixarene. Determined by X-ray diffraction at 2.5 Å resolution. Released 22 Jul 2020.

Method: X-ray diffraction
Resolution: 2.5 Å
Organism: Equus caballus
Chains: 8
Atoms: 7,976
Mol. weight: 108.1 kDa
Ligands: ACE, HEC, 6M7
Released: 22 Jul 2020

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

Secondary structure: helices and β-sheets

6SUV contains 55 α-helices and 16 β-strands across 8 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.

Chains AaA, BaB, CaC, DaD, EaE, FaF and GaG: 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	1
α-helix	50-53	4
β-strand	58	1	1
α-helix	61-69	9
α-helix	71-74	4
α-helix	88-101	14

Chain HaH: 6 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	3-13	11
α-helix	24-26	3
β-strand	39	1	8
α-helix	50-53	4
β-strand	58	1	8
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	AaA, BaB, CaC, DaD, EaE, FaF, GaG, HaH	protein	104	Equus caballus	P00004 (AlphaFold model)

Sequence of entity 1 (AaA, BaB, CaC, DaD, EaE, FaF, GaG, HaH), FASTA

>6SUV_1 Cytochrome c (chains AaA, BaB, CaC, DaD, EaE, FaF, GaG, HaH)
GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWK
EETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE

Ligands and cofactors

ID	Name	Formula	Copies
ACE	Acetyl group	C2 H4 O	8
HEC	Heme C	C34 H36 Fe N4 O4	8
6M7	octa-anionic calixarene	C38 H39 As O25 S4	8

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

Primary citation

Probing the determinants of porosity in protein frameworks: co-crystals of cytochrome c and an octa-anionic calix[4]arene. Alex, J.M., Brancatelli, G., Volpi, S. et al. Org Biomol Chem (2020) 18:211-214. DOI 10.1039/C9OB02275A

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

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