1OCC: Cytochrome C oxidase

Structure of bovine heart cytochrome C oxidase at the fully oxidized state. Determined by X-ray diffraction at 2.8 Å resolution. Released 7 Dec 1996.

Method: X-ray diffraction
Resolution: 2.8 Å
Organism: Bos taurus
Chains: 26
Atoms: 28,722
Mol. weight: 413.61 kDa
Ligands: CU, MG, HEA, ZN
Released: 7 Dec 1996

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

Secondary structure: helices and β-sheets

1OCC contains 192 α-helices and 70 β-strands across 26 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 A and N: 30 helices, 7 β-strands

Element	Residues	Length	Sheet
α-helix	2	1
α-helix	3-7	5
α-helix	12-41	30
α-helix	51-63	13
α-helix	64-70	7
α-helix	71	1
α-helix	72-78	7
α-helix	79-87	9
α-helix	95-115	21
α-helix	141-170	30
α-helix	178-180	3
α-helix	183-212	30
α-helix	222-224	3
α-helix	228-261	34
α-helix	270-283	14
α-helix	288-291	4
α-helix	299-310	12
α-helix	313-327	15
α-helix	336-357	22
α-helix	361-367	7
β-strand	370	1	1
α-helix	371-380	10
α-helix	381-385	5
α-helix	386-401	16
β-strand	403	1	2
α-helix	407-425	19
α-helix	428-433	6
β-strand	437	1	1
α-helix	445-447	3
α-helix	448-478	31
β-strand	481	1	2
β-strand	482-484	3	3
α-helix	488-490	3
α-helix	492-496	5
α-helix	500-501	2
β-strand	510-511	2	4
β-strand	513	1	5

Chains B and O: 8 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	2-3	2
α-helix	9-11	3
α-helix	15-45	31
α-helix	60-87	28
β-strand	95-102	8	6
β-strand	105-110	6	6
β-strand	116-120	5	6
β-strand	122	1	7
α-helix	123-124	2
α-helix	125-127	3
β-strand	138	1	7
β-strand	142-145	4	8
β-strand	150-156	7	6
β-strand	161-165	5	9
α-helix	166-168	3
β-strand	170-174	5	9
β-strand	180-184	5	6
β-strand	190-194	5	8
β-strand	209-214	6	8
α-helix	216-225	10

Chains C and P: 13 helices, 2 β-strands

Element	Residues	Length	Sheet
α-helix	11-13	3
α-helix	16-37	22
α-helix	41-62	22
α-helix	63-67	5
α-helix	73-106	34
α-helix	110-112	3
α-helix	118	1
α-helix	123-125	3
α-helix	129-152	24
α-helix	156-183	28
α-helix	191-223	33
β-strand	228	1	10
β-strand	231	1	10
α-helix	233-252	20
α-helix	253-259	7

Chains D and Q: 10 helices, 4 β-strands

Element	Residues	Length	Sheet
α-helix	8-12	5
β-strand	19	1	11
β-strand	22	1	11
α-helix	35-44	10
α-helix	48-50	3
α-helix	53-63	11
α-helix	68-71	4
α-helix	77-102	26
α-helix	106-108	3
α-helix	109-111	3
α-helix	113-125	13
α-helix	135-137	3
β-strand	138-139	2	12
β-strand	144-145	2	12

Chains E and R: 8 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	8-20	13
α-helix	26-36	11
β-strand	41	1	13
α-helix	42-44	3
α-helix	45-57	13
α-helix	61-74	14
α-helix	81-96	16
α-helix	98-100	3
α-helix	101-104	4

Chains F and S: 5 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	9-12	4
α-helix	15-25	11
α-helix	35-36	2
β-strand	37	1	5
α-helix	38	1
β-strand	47-51	5	14
β-strand	55-60	6	4
α-helix	69	1
β-strand	70-75	6	4
β-strand	80-82	3	14
β-strand	86-93	8	14

Chains G and T: 4 helices, 0 β-strands

Element	Residues	Length
α-helix	13-19	7
α-helix	20-24	5
α-helix	25-37	13
α-helix	45-47	3

Chains H and U: 4 helices, 1 β-strand

Element	Residues	Length	Sheet
α-helix	14-16	3
β-strand	24	1	6
α-helix	26-44	19
α-helix	54-63	10
α-helix	66-78	13

5 more chain groups are not listed. Open the entry in the viewer and use the sequence panel to see them.

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Cytochrome C oxidase	A, N	protein	514	Bos taurus	P00396 (AlphaFold model)
Cytochrome C oxidase	B, O	protein	227	Bos taurus	P68530 (AlphaFold model)
Cytochrome C oxidase	C, P	protein	261	Bos taurus	P00415 (AlphaFold model)
Cytochrome C oxidase	D, Q	protein	147	Bos taurus	P00423 (AlphaFold model)
Cytochrome C oxidase	E, R	protein	109	Bos taurus	P00426
Cytochrome C oxidase	F, S	protein	98	Bos taurus	P00428
Cytochrome C oxidase	G, T	protein	84	Bos taurus	P07471
Cytochrome C oxidase	H, U	protein	85	Bos taurus	P00429
Cytochrome C oxidase	I, V	protein	73	Bos taurus	P04038
Cytochrome C oxidase	J, W	protein	59	Bos taurus	P07470
Cytochrome C oxidase	K, X	protein	56	Bos taurus	P13183
Cytochrome C oxidase	L, Y	protein	47	Bos taurus	P00430

1 more molecules are not listed.

Sequence of entity 1 (A, N), FASTA

>1OCC_1 CYTOCHROME C OXIDASE (chains A, N)
MFINRWLFSTNHKDIGTLYLLFGAWAGMVGTALSLLIRAELGQPGTLLGDDQIYNVVVTA
HAFVMIFFMVMPIMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEA
GAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMSQYQ
TPLFVWSVMITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGH
PEVYILILPGFGMISHIVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGMDVD
TRAYFTSATMIIAIPTGVKVFSWLATLHGGNIKWSPAMMWALGFIFLFTVGGLTGIVLAN
SSLDIVLHDTYYVVAHFHYVLSMGAVFAIMGGFVHWFPLFSGYTLNDTWAKIHFAIMFVG
VNMTFFPQHFLGLSGMPRRYSDYPDAYTMWNTISSMGSFISLTAVMLMVFIIWEAFASKR
EVLTVDLTTTNLEWLNGCPPPYHTFEEPTYVNLK

Sequence of entity 2 (B, O), FASTA

>1OCC_2 CYTOCHROME C OXIDASE (chains B, O)
MAYPMQLGFQDATSPIMEELLHFHDHTLMIVFLISSLVLYIISLMLTTKLTHTSTMDAQE
VETIWTILPAIILILIALPSLRILYMMDEINNPSLTVKTMGHQWYWSYEYTDYEDLSFDS
YMIPTSELKPGELRLLEVDNRVVLPMEMTIRMLVSSEDVLHSWAVPSLGLKTDAIPGRLN
QTTLMSSRPGLYYGQCSEICGSNHSFMPIVLELVPLKYFEKWSASML

Sequence of entity 3 (C, P), FASTA

>1OCC_3 CYTOCHROME C OXIDASE (chains C, P)
MTHQTHAYHMVNPSPWPLTGALSALLMTSGLTMWFHFNSMTLLMIGLTTNMLTMYQWWRD
VIRESTFQGHHTPAVQKGLRYGMILFIISEVLFFTGFFWAFYHSSLAPTPELGGCWPPTG
IHPLNPLEVPLLNTSVLLASGVSITWAHHSLMEGDRKHMLQALFITITLGVYFTLLQASE
YYEAPFTISDGVYGSTFFVATGFHGLHVIIGSTFLIVCFFRQLKFHFTSNHHFGFEAGAW
YWHFVDVVWLFLYVSIYWWGS

Sequence of entity 4 (D, Q), FASTA

>1OCC_4 CYTOCHROME C OXIDASE (chains D, Q)
AHGSVVKSEDYALPSYVDRRDYPLPDVAHVKNLSASQKALKEKEKASWSSLSIDEKVELY
RLKFKESFAEMNRSTNEWKTVVGAAMFFIGFTALLLIWEKHYVYGPIPHTFEEEWVAKQT
KRMLDMKVAPIQGFSAKWDYDKNEWKK

Sequence of entity 5 (E, R), FASTA

>1OCC_5 CYTOCHROME C OXIDASE (chains E, R)
SHGSHETDEEFDARWVTYFNKPDIDAWELRKGMNTLVGYDLVPEPKIIDAALRACRRLND
FASAVRILEVVKDKAGPHKEIYPYVIQELRPTLNELGISTPEELGLDKV

Sequence of entity 6 (F, S), FASTA

>1OCC_6 CYTOCHROME C OXIDASE (chains F, S)
ASGGGVPTDEEQATGLEREVMLAARKGQDPYNILAPKATSGTKEDPNLVPSITNKRIVGC
ICEEDNSTVIWFWLHKGEAQRCPSCGTHYKLVPHQLAH

Sequence of entity 7 (G, T), FASTA

>1OCC_7 CYTOCHROME C OXIDASE (chains G, T)
ASAAKGDHGGTGARTWRFLTFGLALPSVALCTLNSWLHSGHRERPAFIPYHHLRIRTKPF
SWGDGNHTFFHNPRVNPLPTGYEK

Sequence of entity 8 (H, U), FASTA

>1OCC_8 CYTOCHROME C OXIDASE (chains H, U)
AEDIQAKIKNYQTAPFDSRFPNQNQTRNCWQNYLDFHRCEKAMTAKGGDVSVCEWYRRVY
KSLCPISWVSTWDDRRAEGTFPGKI

Sequence of entity 9 (I, V), FASTA

>1OCC_9 CYTOCHROME C OXIDASE (chains I, V)
STALAKPQMRGLLARRLRFHIVGAFMVSLGFATFYKFAVAEKRKKAYADFYRNYDSMKDF
EEMRKAGIFQSAK

Sequence of entity 10 (J, W), FASTA

>1OCC_10 CYTOCHROME C OXIDASE (chains J, W)
FENRVAEKQKLFQEDNGLPVHLKGGATDNILYRVTMTLCLGGTLYSLYCLGWASFPHKK

Sequence of entity 11 (K, X), FASTA

>1OCC_11 CYTOCHROME C OXIDASE (chains K, X)
IHQKRAPDFHDKYGNAVLASGATFCVAVWVYMATQIGIEWNPSPVGRVTPKEWREQ

Sequence of entity 12 (L, Y), FASTA

>1OCC_12 CYTOCHROME C OXIDASE (chains L, Y)
SHYEEGPGKNIPFSVENKWRLLAMMTLFFGSGFAAPFFIVRHQLLKK

Ligands and cofactors

ID	Name	Formula	Copies
CU	Copper (II) ion	Cu	6
MG	Magnesium ion	Mg	2
HEA	Heme-a	C49 H56 Fe N4 O6	4
ZN	Zinc ion	Zn	2

Primary citation

The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8 A. Tsukihara, T., Aoyama, H., Yamashita, E. et al. Science (1996) 272:1136-1144. PubMed

Other PDB entries of the same protein (UniProt P00396 (AlphaFold model), which also has an AlphaFold model), best resolution first:

7COH 1.3 Å, Dimeric Form of Bovine Heart Cytochrome c Oxidase in the Fully Oxidized State
7W3E 1.45 Å, Bovine cytochrome c oxidese in CN-bound fully reduced state at 50 K
5B1A 1.5 Å, Bovine heart cytochrome c oxidase in the fully oxidized state at 1.5 angstrom resolution
7YPY 1.5 Å, Bovine heart cytochrome c oxidase in fully oxidized state at 1.5 angstrom resolution
5B1B 1.6 Å, Bovine heart cytochrome c oxidase in the fully reduced state at 1.6 angstrom resolution
7VUW 1.6 Å, Bovine heart cytochrome c oxidase in the cyanide-bound fully oxidized state at 50 K
9M56 1.6 Å, Bovine Heart Cytochrome c Oxidase in the Fully Reduced State
5ZCP 1.65 Å, azide-bound cytochrome c oxidase structure determined using the crystals exposed to 20…
5ZCQ 1.65 Å, Azide-bound cytochrome c oxidase structure determined using the crystals exposed to 10…
7VVR 1.65 Å, Bovine cytochrome c oxidese in CN-bound mixed valence state at 50 K
5B3S 1.68 Å, Bovine heart cytochrome c oxidase in the carbon monoxide-bound mixed-valence state at…
7EV7 1.7 Å, Bovine heart cytochrome c oxidase in the carbon monoxide-bound fully reduced state at a…

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1OCC is part of these collections:

Metabolism and cellular energy

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