1U75: Cytochrome c peroxidase

Electron Transfer Complex between Horse Heart Cytochrome c and Zinc-Porphyrin Substituted Cytochrome c Peroxidase. Determined by X-ray diffraction at 2.55 Å resolution. Released 28 Sept 2004.

Method: X-ray diffraction
Resolution: 2.55 Å
Organisms: Saccharomyces cerevisiae, Equus caballus
Chains: 3
Atoms: 6,032
Mol. weight: 81.33 kDa
Ligands: ZNH, HEC, PO4
Released: 28 Sept 2004

Explore 1U75 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1U75 contains 50 α-helices and 22 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: 23 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	6-7	2	1
α-helix	16-32	17
α-helix	36-39	4
α-helix	43-54	12
β-strand	58	1	2
β-strand	63	1	2
α-helix	70-72	3
α-helix	74-77	4
α-helix	80-82	3
α-helix	86-98	13
α-helix	104-118	15
β-strand	126	1	3
α-helix	135-137	3
α-helix	138-140	3
α-helix	145-146	2
α-helix	151-159	9
α-helix	165-171	7
α-helix	172-176	5
β-strand	179-180	2	4
α-helix	182-185	4
β-strand	189-190	2	4
α-helix	201-208	8
β-strand	212-215	4	5
β-strand	221-224	4	5
β-strand	230-231	2	5
α-helix	233-240	8
α-helix	242-253	12
α-helix	255-271	17
β-strand	274-275	2	1
α-helix	276	1
α-helix	281-283	3
β-strand	284	1	3
α-helix	286-288	3
α-helix	289-292	4

Chain B: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	6-13	8
α-helix	24-26	3
α-helix	53-55	3
α-helix	88-101	14

Chain C: 23 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	2-4	3
β-strand	7	1	6
α-helix	16-32	17
α-helix	36-39	4
α-helix	43-54	12
β-strand	58	1	7
β-strand	63	1	7
α-helix	70-72	3
α-helix	74-77	4
α-helix	80-82	3
α-helix	86-98	13
α-helix	104-118	15
β-strand	126	1	8
α-helix	135-137	3
α-helix	138-140	3
α-helix	145-146	2
α-helix	151-159	9
α-helix	165-171	7
α-helix	172-176	5
β-strand	179-180	2	9
α-helix	182-185	4
β-strand	189-190	2	9
α-helix	201-208	8
β-strand	211-215	5	10
β-strand	221-225	5	10
β-strand	230-231	2	10
α-helix	233-236	4
α-helix	242-253	12
α-helix	255-271	17
β-strand	275	1	6
α-helix	276-277	2
α-helix	280-283	4
β-strand	284	1	8
α-helix	286-288	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
cytochrome c peroxidase	A, C	protein	296	Saccharomyces cerevisiae	P00431 (AlphaFold model)
Cytochrome c	B	protein	104	Equus caballus	P00004 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1U75_1 cytochrome c peroxidase (chains A, C)
MITTPLVHVASVEKGRSYEDFQKVYNAIALKLREDDEYDNYIGYGPVLVRLAWHISGTWD
KHDNTGGSYGGTYRFKKEFNDPSNAGLQNGFKFLEPIHKEFPWISSGDLFSLGGVTAVQE
MQGPKIPWRCGRVDTPEDTTPDNGRLPDADKDAGYVRTFFQRLNMNDREVVALMGAHALG
KTHLKNSGYEGPWGAANNVFTNEFYLNLLNEDWKLEKNDANNEQWDSKSGYMMLPTDYSL
IQDPKYLSIVKEYANDQDKFFKDFSKAFEKLLENGITFPKDAPSPFIFKTLEEQGL

Sequence of entity 2 (B), FASTA

>1U75_2 Cytochrome c (chains B)
GDVEKGKKIFVQKCAQCHTVEKGGKHKTGPNLHGLFGRKTGQAPGFTYTDANKNKGITWK
EETLMEYLENPKKYIPGTKMIFAGIKKKTEREDLIAYLKKATNE

Ligands and cofactors

ID	Name	Formula	Copies
ZNH	Protoporphyrin IX containing ZN	C34 H32 N4 O4 Zn	2
HEC	Heme C	C34 H36 Fe N4 O4	1
PO4	Phosphate ion	O4 P	2

Primary citation

Electron transfer between cytochrome c and cytochome c peroxidase in single crystals. Kang, S.A., Marjavaara, P.J., Crane, B.R. J Am Chem Soc (2004) 126:10836-10837. DOI 10.1021/ja049230u · 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
3E2N 1.3 Å, Engineering ascorbate peroxidase activity into cytochrome c peroxidase
2AQD 1.35 Å, cytochrome c peroxidase (CCP) in complex with 2,5-diaminopyridine

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