3E2N: Cytochrome c peroxidase

Engineering ascorbate peroxidase activity into cytochrome c peroxidase. Determined by X-ray diffraction at 1.3 Å resolution. Released 21 Oct 2008.

Method: X-ray diffraction
Resolution: 1.3 Å
Organisms: Saccharomyces cerevisiae, Pisum sativum
Chains: 1
Atoms: 2,910
Mol. weight: 33.22 kDa
Ligands: HEM
Released: 21 Oct 2008

Explore 3E2N in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3E2N contains 22 α-helices and 11 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: 22 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	7	1	1
α-helix	10-11	2
α-helix	16-33	18
α-helix	36-47	12
β-strand	51	1	2
β-strand	56	1	2
α-helix	63-65	3
α-helix	67-70	4
α-helix	73-75	3
α-helix	78-91	14
α-helix	97-111	15
β-strand	119	1	3
α-helix	128-130	3
α-helix	131-133	3
α-helix	138-139	2
α-helix	144-152	9
α-helix	158-165	8
α-helix	166-170	5
β-strand	172-173	2	4
α-helix	175-178	4
β-strand	182-183	2	4
α-helix	194-201	8
β-strand	204-208	5	5
β-strand	214-218	5	5
β-strand	223-224	2	5
α-helix	226-233	8
α-helix	235-245	11
α-helix	248-264	17
β-strand	268	1	1
α-helix	274-276	3
β-strand	277	1	3
α-helix	279-281	3
α-helix	282-285	4

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cytochrome c peroxidase	A	protein	287	Saccharomyces cerevisiae, Pisum sativum	P00431 (AlphaFold model), P48534 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>3E2N_1 Cytochrome c peroxidase (chains A)
TTPLVHVASVEKGRSYEDFQKVYNAIALKIAEKKCGPVLVRLAWHTSGTWDKHDNTGGSY
GGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQEMQGPKIPWR
CGRVDTPEDTTPDNGRLPDADKDADYVRTFFQRLNMNDREVVALMGAHALGKTHLKRSGY
EGPFGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSLIQDPKYLSI
VKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL

Ligands and cofactors

ID	Name	Formula	Copies
HEM	Protoporphyrin IX containing FE	C34 H32 Fe N4 O4	1

Primary citation

Engineering ascorbate peroxidase activity into cytochrome c peroxidase. Meharenna, Y.T., Oertel, P., Bhaskar, B. et al. Biochemistry (2008) 47:10324-10332. DOI 10.1021/bi8007565 · PubMed

Other PDB entries of the same protein (UniProt P00431 (AlphaFold model), which also has an AlphaFold model), best resolution first:

3E2O 1.06 Å, Crystal structure of cytochrome c peroxidase, N184R mutant
7BIU 1.06 Å, XFEL crystal structure of cytochrome c peroxidase compound II
2EUT 1.12 Å, Cytochrome c peroxidase (CCP) in complex with 2-amino-4-picoline
1Z53 1.13 Å, The 1.13 Angstrom Structure of Iron-free Cytochrome c Peroxidase
1ZBY 1.2 Å, High-Resolution Crystal Structure of Native (Resting) Cytochrome c Peroxidase (CcP)
2RBT 1.24 Å, n-methylbenzylamine in complex with Cytochrome C Peroxidase W191G
2Y5A 1.25 Å, Cytochrome c peroxidase (CCP) W191G bound to 3-aminopyridine
1ZBZ 1.29 Å, High-Resolution Crystal Structure of Compound I intermediate of Cytochrome c Peroxidase…
2AS4 1.3 Å, cytochrome c peroxidase in complex with 3-fluorocatechol
2EUQ 1.3 Å, Cytochrome c peroxydase (CCP) in complex with 3-thienylmethylamine
2AQD 1.35 Å, cytochrome c peroxidase (CCP) in complex with 2,5-diaminopyridine
2EUR 1.39 Å, Cytochrome c peroxidase (CCP) in complex with 4-pyridylcarbinol

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